Journal articles: 'Mechanical properties of protein materials'

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Kumar, Rakesh, Linxiang Wang, and Lina Zhang. "Structure and mechanical properties of soy protein materials plasticized by Thiodiglycol." Journal of Applied Polymer Science 111, no. 2 (October 17, 2008): 970–77. http://dx.doi.org/10.1002/app.29136.

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Ford, Audrey C., Hans Machula, Robert S. Kellar, and Brent A. Nelson. "Characterizing the mechanical properties of tropoelastin protein scaffolds." MRS Proceedings 1569 (2013): 45–50. http://dx.doi.org/10.1557/opl.2013.1059.

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ABSTRACTThis paper reports on mechanical characterization of electrospun tissue scaffolds formed from varying blends of collagen and human tropoelastin. The electrospun tropoelastin-based scaffolds have an open, porous structure conducive to cell attachment and have been shown to exhibit strong biocompatibility, but the mechanical character is not well known. Mechanical properties were tested for scaffolds consisting of 100% tropoelastin and 1:1 tropoelastin-collagen blends. The results showed that the materials exhibited a three order of magnitude change in the initial elastic modulus when tested dry vs. hydrated, with moduli of 21 MPa and 0.011 MPa respectively. Noncrosslinked and crosslinked tropoelastin scaffolds exhibited the same initial stiffness from 0 to 50% strain, and the noncrosslinked scaffolds exhibited no stiffness at strains >∼50%. The elastic modulus of a 1:1 tropoelastin-collagen blend was 50% higher than that of a pure tropoelastin scaffold. Finally, the 1:1 tropoelastin-collagen blend was five times stiffer from 0 to 50% strain when strained at five times the ASTM standard rate. By systematically varying protein composition and crosslinking, the results demonstrate how protein scaffolds might be manipulated as customized biomaterials, ensuring mechanical robustness and potentially improving biocompatibility through minimization of compliance mismatch with the surrounding tissue environment. Moreover, the demonstration of strain-rate dependent mechanical behavior has implications for mechanical design of tropoelastin-based tissue scaffolds.

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Gosline, John M. "Structure and Mechanical Properties of Rubberlike Proteins in Animals." Rubber Chemistry and Technology 60, no. 3 (July 1, 1987): 417–38. http://dx.doi.org/10.5254/1.3536137.

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Abstract Polymer networks formed from protein molecules that adopt kinetically-free, random-coil conformations are found in many animals, where they play a number of important roles. The 5 rubberlike proteins isolated and studied to date indicate that animal rubbers, like their synthetic counterparts, contain random networks which are usually stabilized by covalent crosslinks. Long-range elasticity in rubberlike proteins is based on changes in the conformational entropy of random-coil molecules. Further, these protein networks show viscoelastic glass transitions similar to all other amorphous polymer networks. Future research on protein sequences should increase our understanding of how polypeptide chains can function as random-coil molecules, and studies into the mechanical state of elastin in arterial tissues may provide important clues about the mechanisms of some forms of human disease.

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Buchko, Christopher J., Margaret J. Slattery, Kenneth M. Kozloff, and David C. Martin. "Mechanical properties of biocompatible protein polymer thin films." Journal of Materials Research 15, no. 1 (January 2000): 231–42. http://dx.doi.org/10.1557/jmr.2000.0038.

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A silklike protein with fibronectin functionality (SLPF) (ProNectin F®, Protein Polymer Technologies, Inc.) is a genetically engineered protein polymer containing structural and biofunctional segments. The mechanical properties and deformation mechanisms of electrostatically deposited SLPF thin films were examined by scratch testing, tensile testing, and nanoindentation. Scanning electron microscopy and scanned probe microscopy revealed that the macroscopic properties were a sensitive function of microstructure. The SLPF films were relatively brittle in tension, with typical elongation-to-break values of 3%. Nanoindentation data were fit to a power law relationship.

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Gosline, J., M. Lillie, E. Carrington, P. Guerette, C. Ortlepp, and K. Savage. "Elastic proteins: biological roles and mechanical properties." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1418 (February 28, 2002): 121–32. http://dx.doi.org/10.1098/rstb.2001.1022.

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The term ‘elastic protein’ applies to many structural proteins with diverse functions and mechanical properties so there is room for confusion about its meaning. Elastic implies the property of elasticity, or the ability to deform reversibly without loss of energy; so elastic proteins should have high resilience. Another meaning for elastic is ‘stretchy’, or the ability to be deformed to large strains with little force. Thus, elastic proteins should have low stiffness. The combination of high resilience, large strains and low stiffness is characteristic of rubber–like proteins (e.g. resilin and elastin) that function in the storage of elastic–strain energy. Other elastic proteins play very different roles and have very different properties. Collagen fibres provide exceptional energy storage capacity but are not very stretchy. Mussel byssus threads and spider dragline silks are also elastic proteins because, in spite of their considerable strength and stiffness, they are remarkably stretchy. The combination of strength and extensibility, together with low resilience, gives these materials an impressive resistance to fracture (i.e. toughness), a property that allows mussels to survive crashing waves and spiders to build exquisite aerial filters. Given this range of properties and functions, it is probable that elastic proteins will provide a wealth of chemical structures and elastic mechanisms that can be exploited in novel structural materials through biotechnology.

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Folegatti, Marília I. S., Aloísio José Antunes, and Jorge A. Marcondes. "Mechanical and permeability properties of milk protein films." Brazilian Archives of Biology and Technology 41, no. 3 (1998): 320–28. http://dx.doi.org/10.1590/s1516-89131998000300008.

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Edible films present a potential alternative for replacing plastic films used for packaging in food industry. One of the major advantages is the environmental appeal of this technology, which produces no packaging waste. Some films made with other edible materials have found commercial applications, and many more are being developed using a myriad of food based components. This paper focuses on some important characteristics of films produced with sodium and calcium caseinates. The effects of caseinate type and concentration, plasticizer concentration and pH were studied. Major parameters investigated were solubility, tensile properties, water vapour and oxygen permeabilities. Caseinate films showed high solubility at pH range 6.0-8.0 and complete insolubility at pH 3.0 and 4.0. Calcium caseinate films had a higher tensile strength and a lower % elongation at break than sodium caseinate films. There was not significant difference in water vapour and oxygen permeabilities between sodium and calcium caseinate films.

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Tsai, Shang-Pu, David W. Howell, Zhao Huang, Hao-Ching Hsiao, Yang Lu, Kathleen S. Matthews, Jun Lou, and Sarah E. Bondos. "The Effect of Protein Fusions on the Production and Mechanical Properties of Protein-Based Materials." Advanced Functional Materials 25, no. 9 (January 27, 2015): 1442–50. http://dx.doi.org/10.1002/adfm.201402997.

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Jong, L. "Dynamic Mechanical Properties of Soy Protein Filled Elastomers." Journal of Polymers and the Environment 13, no. 4 (October 2005): 329–38. http://dx.doi.org/10.1007/s10924-005-5526-z.

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Sato, M., W. H. Schwartz, S. C. Selden, and T. D. Pollard. "Mechanical properties of brain tubulin and microtubules." Journal of Cell Biology 106, no. 4 (April 1, 1988): 1205–11. http://dx.doi.org/10.1083/jcb.106.4.1205.

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We measured the elasticity and viscosity of brain tubulin solutions under various conditions with a cone and plate rheometer using both oscillatory and steady shearing modes. Microtubules composed of purified tubulin, purified tubulin with taxol and 3x cycled microtubule protein from pig, cow, and chicken behaved as mechanically indistinguishable viscoelastic materials. Microtubules composed of pure tubulin and heat stable microtubule-associated proteins were also similar but did not recover their mechanical properties after shearing like other samples, even after 60 min. All of the other microtubule samples were more rigid after flow orientation, suggesting that the mechanical properties of anisotropic arrays of microtubules may be substantially greater than those of randomly arranged microtubules. These experiments confirm that MAPs do not cross link microtubules. Surprisingly, under conditions where microtubule assembly is strongly inhibited (either 5 degrees or at 37 degrees C with colchicine or Ca++) tubulin was mechanically indistinguishable from microtubules at 10-20 microM concentration. By electron microscopy and ultracentrifugation these samples were devoid of microtubules or other obvious structures. However, these mechanical data are strong evidence that tubulin will spontaneously assemble into alternate structures (aggregates) in nonpolymerizing conditions. Because unpolymerized tubulin is found in significant quantities in the cytoplasm, it may contribute significantly to the viscoelastic properties of cytoplasm, especially at low deformation rates.

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Xue, Ye, Samuel Lofland, and Xiao Hu. "Thermal Conductivity of Protein-Based Materials: A Review." Polymers 11, no. 3 (March 11, 2019): 456. http://dx.doi.org/10.3390/polym11030456.

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Fibrous proteins such as silks have been used as textile and biomedical materials for decades due to their natural abundance, high flexibility, biocompatibility, and excellent mechanical properties. In addition, they also can avoid many problems related to traditional materials such as toxic chemical residues or brittleness. With the fast development of cutting-edge flexible materials and bioelectronics processing technologies, the market for biocompatible materials with extremely high or low thermal conductivity is growing rapidly. The thermal conductivity of protein films, which is usually on the order of 0.1 W/m·K, can be rather tunable as the value for stretched protein fibers can be substantially larger, outperforming that of many synthetic polymer materials. These findings indicate that the thermal conductivity and the heat transfer direction of protein-based materials can be finely controlled by manipulating their nano-scale structures. This review will focus on the structure of different fibrous proteins, such as silks, collagen and keratin, summarizing factors that can influence the thermal conductivity of protein-based materials and the different experimental methods used to measure their heat transfer properties.

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Bealer, Elizabeth J., Kyril Kavetsky, Sierra Dutko, Samuel Lofland, and Xiao Hu. "Protein and Polysaccharide-Based Magnetic Composite Materials for Medical Applications." International Journal of Molecular Sciences 21, no. 1 (December 26, 2019): 186. http://dx.doi.org/10.3390/ijms21010186.

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The combination of protein and polysaccharides with magnetic materials has been implemented in biomedical applications for decades. Proteins such as silk, collagen, and elastin and polysaccharides such as chitosan, cellulose, and alginate have been heavily used in composite biomaterials. The wide diversity in the structure of the materials including their primary monomer/amino acid sequences allow for tunable properties. Various types of these composites are highly regarded due to their biocompatible, thermal, and mechanical properties while retaining their biological characteristics. This review provides information on protein and polysaccharide materials combined with magnetic elements in the biomedical space showcasing the materials used, fabrication methods, and their subsequent applications in biomedical research.

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Gioia, Lodovico di, Bernard Cuq, and Stéphane Guilbert. "Mechanical and water barrier properties of corn-protein-based biodegradable plastics." Journal of Materials Research 15, no. 12 (December 2000): 2612–19. http://dx.doi.org/10.1557/jmr.2000.0375.

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Experiments were performed to evaluate the mechanical and water barrier properties of corn-protein-based materials that were compression molded from thermoplastic resins. The influence of varying concentrations of water, glycerol, and octanoic acid was studied. At 0% relative humidity, the material exhibited a linear elastic deformation and a brittle fracture at any glycerol or octanoic acid content. Raising relative humidity from 0% to 97.3%, progressively decreased the tensile strength (from 24.1 to 2.2 MPa and 19.4 to 1.0 MPa), and the modulus of elasticity (from 1.67 to 0.03 GPa and 1.87 to 0.13 GPa), respectively, for the octanoic acid- or glycerol-plasticized materials. Increasing water content did not increase the tensile strain at break of the glycerol-plasticized material, whereas this parameter changed from 1.6 to 52.3% for octanoic-acid-plasticized material. This last material was waterproof during 21 h and its water transmission rate was then 0.05 mmolmm-2 s -1. Differences in water absorption were related to plasticizer solubility and material structure.

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Huerta-López, Carla, and Jorge Alegre-Cebollada. "Protein Hydrogels: The Swiss Army Knife for Enhanced Mechanical and Bioactive Properties of Biomaterials." Nanomaterials 11, no. 7 (June 24, 2021): 1656. http://dx.doi.org/10.3390/nano11071656.

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Biomaterials are dynamic tools with many applications: from the primitive use of bone and wood in the replacement of lost limbs and body parts, to the refined involvement of smart and responsive biomaterials in modern medicine and biomedical sciences. Hydrogels constitute a subtype of biomaterials built from water-swollen polymer networks. Their large water content and soft mechanical properties are highly similar to most biological tissues, making them ideal for tissue engineering and biomedical applications. The mechanical properties of hydrogels and their modulation have attracted a lot of attention from the field of mechanobiology. Protein-based hydrogels are becoming increasingly attractive due to their endless design options and array of functionalities, as well as their responsiveness to stimuli. Furthermore, just like the extracellular matrix, they are inherently viscoelastic in part due to mechanical unfolding/refolding transitions of folded protein domains. This review summarizes different natural and engineered protein hydrogels focusing on different strategies followed to modulate their mechanical properties. Applications of mechanically tunable protein-based hydrogels in drug delivery, tissue engineering and mechanobiology are discussed.

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Erdohan, Z. Özge, and K. Nazan Turhan. "Barrier and mechanical properties of methylcellulose-whey protein films." Packaging Technology and Science 18, no. 6 (2005): 295–302. http://dx.doi.org/10.1002/pts.700.

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Panahandeh, Sanaz, Siyu Li, and Roya Zandi. "The equilibrium structure of self-assembled protein nano-cages." Nanoscale 10, no. 48 (2018): 22802–9. http://dx.doi.org/10.1039/c8nr07202g.

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Sun, Jing, Juanjuan Su, Chao Ma, Robert Göstl, Andreas Herrmann, Kai Liu, and Hongjie Zhang. "Fabrication and Mechanical Properties of Engineered Protein‐Based Adhesives and Fibers." Advanced Materials 32, no. 6 (December 5, 2019): 1906360. http://dx.doi.org/10.1002/adma.201906360.

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Yuvienco, Carlo, Haresh T. More, Jennifer S. Haghpanah, Raymond S. Tu, and Jin Kim Montclare. "Modulating Supramolecular Assemblies and Mechanical Properties of Engineered Protein Materials by Fluorinated Amino Acids." Biomacromolecules 13, no. 8 (July 24, 2012): 2273–78. http://dx.doi.org/10.1021/bm3005116.

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Zhou, Ming-Liang, Zhi-Gang Qian, Liang Chen, David L. Kaplan, and Xiao-Xia Xia. "Rationally Designed Redox-Sensitive Protein Hydrogels with Tunable Mechanical Properties." Biomacromolecules 17, no. 11 (October 11, 2016): 3508–15. http://dx.doi.org/10.1021/acs.biomac.6b00973.

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Jahangirian, Azizi, Rafiee-Moghaddam, Baratvand, and Webster. "Status of Plant Protein-Based Green Scaffolds for Regenerative Medicine Applications." Biomolecules 9, no. 10 (October 17, 2019): 619. http://dx.doi.org/10.3390/biom9100619.

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In recent decades, regenerative medicine has merited substantial attention from scientific and research communities. One of the essential requirements for this new strategy in medicine is the production of biocompatible and biodegradable scaffolds with desirable geometric structures and mechanical properties. Despite such promise, it appears that regenerative medicine is the last field to embrace green, or environmentally-friendly, processes, as many traditional tissue engineering materials employ toxic solvents and polymers that are clearly not environmentally friendly. Scaffolds fabricated from plant proteins (for example, zein, soy protein, and wheat gluten), possess proper mechanical properties, remarkable biocompatibility and aqueous stability which make them appropriate green biomaterials for regenerative medicine applications. The use of plant-derived proteins in regenerative medicine has been especially inspired by green medicine, which is the use of environmentally friendly materials in medicine. In the current review paper, the literature is reviewed and summarized for the applicability of plant proteins as biopolymer materials for several green regenerative medicine and tissue engineering applications.

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Ku Marsilla, K. I., and Casparus J. R. Verbeek. "Mechanical Properties of Thermoplastic Protein From Bloodmeal and Polyester Blends." Macromolecular Materials and Engineering 299, no. 7 (February 27, 2014): 885–95. http://dx.doi.org/10.1002/mame.201300396.

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Lei, Duo, and Xiaojun Ma. "Effect of enzymatic glycosylation on the structure and properties of wheat gluten protein fibers." Journal of Engineered Fibers and Fabrics 16 (January 2021): 155892502110003. http://dx.doi.org/10.1177/15589250211000337.

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Wheat gluten proteins are good raw materials for preparing fibers due to their excellent viscoelasticity. However, protein fibers made directly from wheat gluten have poor mechanical properties. In this paper, transglutaminase was used to induce the glycosylation reaction between wheat gluten proteins and carboxymethyl chitosan. The glycated proteins were then made into fibers by wet spinning. After glycosylation modification, the breaking strength and breaking elongation of the wheat gluten protein fibers (WGPF) improved by 43% and 127%, respectively. Fourier transform infrared spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses revealed that the glycosylation-modified WGPF molecules contained saccharide portions, which confirms the covalent attachment of carboxymethyl chitosan to the wheat gluten protein. Scanning electron microscopy showed that the number of pores in the cross-section of the modified WGPF was lower than that in the unmodified WGPF. The thermal stability and dyeability of the modified WGPF were also improved.

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Greco, Gabriele, and Nicola M. Pugno. "Mechanical Properties and Weibull Scaling Laws of Unknown Spider Silks." Molecules 25, no. 12 (June 26, 2020): 2938. http://dx.doi.org/10.3390/molecules25122938.

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Spider silks present extraordinary mechanical properties, which have attracted the attention of material scientists in recent decades. In particular, the strength and the toughness of these protein-based materials outperform the ones of many man-made fibers. Unfortunately, despite the huge interest, there is an absence of statistical investigation on the mechanical properties of spider silks and their related size effects due to the length of the fibers. Moreover, several spider silks have never been mechanically tested. Accordingly, in this work, we measured the mechanical properties and computed the Weibull parameters for different spider silks, some of them unknown in the literature. We also measured the mechanical properties at different strain rates for the dragline of the species Cupiennius salei. For the same species, we measured the strength and Weibull parameters at different fiber lengths. In this way, we obtained the spider silk scaling laws directly and according to Weibull’s prediction. Both length and strain rates affect the mechanical properties of spider silk, as rationalized by Weibull’s statistics.

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Jagannath, J. H., C. Nanjappa, D. K. Das Gupta, and A. S. Bawa. "Mechanical and barrier properties of edible starch-protein-based films." Journal of Applied Polymer Science 88, no. 1 (January 27, 2003): 64–71. http://dx.doi.org/10.1002/app.11602.

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Schmid, Markus, Kerstin Dallmann, Elodie Bugnicourt, Dario Cordoni, Florian Wild, Andrea Lazzeri, and Klaus Noller. "Properties of Whey-Protein-Coated Films and Laminates as Novel Recyclable Food Packaging Materials with Excellent Barrier Properties." International Journal of Polymer Science 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/562381.

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In case of food packaging applications, high oxygen and water vapour barriers are the prerequisite conditions for preserving the quality of the products throughout their whole lifecycle. Currently available polymers and/or biopolymer films are mostly used in combination with barrier materials derived from oil based plastics or aluminium to enhance their low barrier properties. In order to replace these non-renewable materials, current research efforts are focused on the development of sustainable coatings, while maintaining the functional properties of the resulting packaging materials. This article provides an introduction to food packaging requirements, highlights prior art on the use of whey-based coatings for their barriers properties, and describes the key properties of an innovative packaging multilayer material that includes a whey-based layer. The developed whey protein formulations had excellent barrier properties almost comparable to the ethylene vinyl alcohol copolymers (EVOH) barrier layer conventionally used in food packaging composites, with an oxygen barrier (OTR) of <2 [cm³(STP)/(m²d bar)] when normalized to a thickness of 100 μm. Further requirements of the barrier layer are good adhesion to the substrate and sufficient flexibility to withstand mechanical load while preventing delamination and/or brittle fracture. Whey-protein-based coatings have successfully met these functional and mechanical requirements.

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Choi, Bumjoon, Taehee Kim, Sang Woo Lee, and Kilho Eom. "Nanomechanical Characterization of Amyloid Fibrils Using Single-Molecule Experiments and Computational Simulations." Journal of Nanomaterials 2016 (2016): 1–16. http://dx.doi.org/10.1155/2016/5873695.

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Amyloid fibrils have recently received much attention due to not only their important role in disease pathogenesis but also their excellent mechanical properties, which are comparable to those of mechanically strong protein materials such as spider silk. This indicates the necessity of understanding fundamental principles providing insight into how amyloid fibrils exhibit the excellent mechanical properties, which may allow for developing biomimetic materials whose material (e.g., mechanical) properties can be controlled. Here, we describe recent efforts to characterize the nanomechanical properties of amyloid fibrils using computational simulations (e.g., atomistic simulations) and single-molecule experiments (e.g., atomic force microscopy experiments). This paper summarizes theoretical models, which are useful in analyzing the mechanical properties of amyloid fibrils based on simulations and experiments, such as continuum elastic (beam) model, elastic network model, and polymer statistical model. In this paper, we suggest how the nanomechanical properties of amyloid fibrils can be characterized and determined using computational simulations and/or atomic force microscopy experiments coupled with the theoretical models.

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Tahsiri, Zahra, Hamideh Mirzaei, Seyed Mohammad Hashem Hosseini, and Mohammadreza Khalesi. "Gum arabic improves the mechanical properties of wild almond protein film." Carbohydrate Polymers 222 (October 2019): 114994. http://dx.doi.org/10.1016/j.carbpol.2019.114994.

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Gofferje, Gabriele, Markus Schmid, and Andreas Stäbler. "Characterization ofJatropha curcasL. Protein Cast Films with respect to Packaging Relevant Properties." International Journal of Polymer Science 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/630585.

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There is increasing research ongoing towards the substitution of petrochemical based plastics by more sustainable raw materials, especially in the field of bioplastics. Proteins of different types such as whey, casein, gelatine, or zein show potential beyond the food and feed industry as, for instance, the application in packaging. Protein based coatings provide different packaging relevant properties such as barrier against permanent gases, certain water vapour barrier, and mechanical resistance. The aim of this study was to explore the potential for packaging applications of proteins fromJatropha curcasL. and to compare the performance with literature data on cast films from whey protein isolate. As a by-product from oil extraction, high amounts ofJatrophameal are obtained requiring a concept for its sustainable utilization.Jatrophaseed cake includes up to 40% (w/w) of protein which is currently not utilized. The present study provides new data on the potential ofJatrophaprotein for packaging applications. It was shown thatJatrophaprotein cast films show suitable barrier and mechanical properties depending on the extraction and purification method as well as on the plasticiser content. Based on these findingsJatrophaproteins own potential to be utilized as coating material for food packaging applications.

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Chen, Hongbo, Jingjing Wang, Yaohua Cheng, Chuansheng Wang, Haichao Liu, Huiguang Bian, Yiren Pan, Jingyao Sun, and Wenwen Han. "Application of Protein-Based Films and Coatings for Food Packaging: A Review." Polymers 11, no. 12 (December 9, 2019): 2039. http://dx.doi.org/10.3390/polym11122039.

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As the IV generation of packaging, biopolymers, with the advantages of biodegradability, process ability, combination possibilities and no pollution to food, have become the leading food packaging materials. Biopolymers can be directly extracted from biomass, synthesized from bioderived monomers and produced directly by microorganisms which are all abundant and renewable. The raw materials used to produce biopolymers are low-cost, some even coming from agrion dustrial waste. This review summarized the advances in protein-based films and coatings for food packaging. The materials studied to develop protein-based packaging films and coatings can be divided into two classes: plant proteins and animal proteins. Parts of proteins are referred in this review, including plant proteins i.e., gluten, soy proteins and zein, and animal proteins i.e., casein, whey and gelatin. Films and coatings based on these proteins have excellent gas barrier properties and satisfactory mechanical properties. However, the hydrophilicity of proteins makes the protein-based films present poor water barrier characteristics. The application of plasticizers and the corresponding post-treatments can make the properties of the protein-based films and coatings improved. The addition of active compounds into protein-based films can effectively inhibit or delay the growth of microorganisms and the oxidation of lipids. The review also summarized the research about the storage requirements of various foods that can provide corresponding guidance for the preparation of food packaging materials. Numerous application examples of protein-based films and coatings in food packaging also confirm their important role in food packaging materials.

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Terrié, C., V. Constantinescu, N. Leblanc, and J. M. Saiter. "Influence of Proteins on the Mechanical Properties of Agro-Based Materials." Macromolecular Symposia 296, no. 1 (October 2010): 617–21. http://dx.doi.org/10.1002/masy.201051080.

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van der Sleen, Lyan M., and Katarzyna M. Tych. "Bioconjugation Strategies for Connecting Proteins to DNA-Linkers for Single-Molecule Force-Based Experiments." Nanomaterials 11, no. 9 (September 17, 2021): 2424. http://dx.doi.org/10.3390/nano11092424.

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The mechanical properties of proteins can be studied with single molecule force spectroscopy (SMFS) using optical tweezers, atomic force microscopy and magnetic tweezers. It is common to utilize a flexible linker between the protein and trapped probe to exclude short-range interactions in SMFS experiments. One of the most prevalent linkers is DNA due to its well-defined properties, although attachment strategies between the DNA linker and protein or probe may vary. We will therefore provide a general overview of the currently existing non-covalent and covalent bioconjugation strategies to site-specifically conjugate DNA-linkers to the protein of interest. In the search for a standardized conjugation strategy, considerations include their mechanical properties in the context of SMFS, feasibility of site-directed labeling, labeling efficiency, and costs.

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Stephanopoulos, Nicholas, and Petr Šulc. "DNA Nanodevices as Mechanical Probes of Protein Structure and Function." Applied Sciences 11, no. 6 (March 21, 2021): 2802. http://dx.doi.org/10.3390/app11062802.

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DNA nanotechnology has reported a wide range of structurally tunable scaffolds with precise control over their size, shape and mechanical properties. One promising application of these nanodevices is as probes for protein function or determination of protein structure. In this perspective we cover several recent examples in this field, including determining the effect of ligand spacing and multivalency on cell activation, applying forces at the nanoscale, and helping to solve protein structure by cryo-EM. We also highlight some future directions in the chemistry necessary for integrating proteins with DNA nanoscaffolds, as well as opportunities for computational modeling of hybrid protein-DNA nanomaterials.

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Zhou, Ziyan, Hua Zheng, Ming Wei, Jin Huang, and Yun Chen. "Structure and mechanical properties of cellulose derivatives/soy protein isolate blends." Journal of Applied Polymer Science 107, no. 5 (2007): 3267–74. http://dx.doi.org/10.1002/app.27323.

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Prochoń, Mirosława, and Anita Przepiórkowska. "Innovative Application of Biopolymer Keratin as a Filler of Synthetic Acrylonitrile-Butadiene Rubber NBR." Journal of Chemistry 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/787269.

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The current investigations show the influence of keratin, recovered from the tanning industry, on the thermal and mechanical properties of vulcanizates with synthetic rubber acrylonitrile-butadiene rubber NBR. The addition of waste protein to NBR vulcanizates influences the improvement of resistance at high temperatures and mechanical properties like tensile strength and hardness. The introduction of keratin to the mixes of rubber previously blended with zinc oxide (ZnO) before vulcanization process leads to an increase in the cross-linking density of vulcanizates. The polymer materials received including addition of proteins will undergo biodecomposition in natural conditions. After soil test, vulcanizates with keratin especially keratin with ZnO showed much more changes on the surface area than vulcanizates without protein. In that aerobic environment, microorganisms, bacteria, and fungus digested better polymer materials containing natural additives.

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Becerra, Natalia Y., Luz M. Restrepo, Yessika Galeano, Ana C. Tobón, Luis F. Turizo, and Monica Mesa. "Improving Fibrin Hydrogels’ Mechanical Properties, through Addition of Silica or Chitosan-Silica Materials, for Potential Application as Wound Dressings." International Journal of Biomaterials 2021 (June 2, 2021): 1–11. http://dx.doi.org/10.1155/2021/9933331.

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Fibrin is a protein-based hydrogel formed during blood coagulation. It can also be produced in vitro from human blood plasma, and it is capable of resisting high deformations. However, after each deformation process, it loses high amounts of water, which subsequently makes it mechanically unstable and, finally, difficult to manipulate. The objective of this work was to overcome the in vitro fibrin mechanical instability. The strategy consists of adding silica or chitosan-silica materials and comparing how the different materials electrokinetic-surface properties affect the achieved improvement. The siliceous materials electrostatic and steric stabilization mechanisms, together with plasma protein adsorption on their surfaces, were corroborated by DLS and ζ-potential measurements before fibrin gelling. These properties avoid phase separation, favoring homogeneous incorporation of the solid into the forming fibrin network. Young’s modulus of modified fibrin hydrogels was evaluated by AFM to quantitatively measure stiffness. It increased 2.5 times with the addition of 4 mg/mL silica. A similar improvement was achieved with only 0.7 mg/mL chitosan-silica, which highlighted the contribution of hydrophilic chitosan chains to fibrinogen crosslinking. Moreover, these chains avoided the fibroblast growth inhibition onto modified fibrin hydrogels 3D culture observed with silica. In conclusion, 0.7 mg/mL chitosan-silica improved the mechanical stability of fibrin hydrogels with low risks of cytotoxicity. This easy-to-manipulate modified fibrin hydrogel makes it suitable as a wound dressing biomaterial.

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Cheng, Yun-hui, Zhang Wang, and Shi-ying Xu. "Antioxidant properties of wheat germ protein hydrolysates evaluated in vitro." Journal of Central South University of Technology 13, no. 2 (April 2006): 160–65. http://dx.doi.org/10.1007/s11771-006-0149-7.

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Kwon, Kwang-Jun, and Hyun Seok. "Silk Protein-Based Membrane for Guided Bone Regeneration." Applied Sciences 8, no. 8 (July 24, 2018): 1214. http://dx.doi.org/10.3390/app8081214.

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Silk derived from the silkworm is known for its excellent biological and mechanical properties. It has been used in various fields as a biomaterial, especially in bone tissue engineering scaffolding. Recently, silk protein-based biomaterial has been used as a barrier membrane scaffolding for guided bone regeneration (GBR). GBR promotes bone regeneration in bone defect areas using special barrier membranes. GBR membranes should have biocompatibility, biodegradability, cell occlusion, the mechanical properties of space-making, and easy clinical handling. Silk-based biomaterial has excellent biologic and mechanical properties that make it a good candidate to be used as GBR membranes. Recently, various forms of silk protein-based membranes have been introduced, demonstrating excellent bone regeneration ability, including osteogenic cell proliferation and osteogenic gene expression, and promoting new bone regeneration in vivo. In this article, we introduced the characteristics of silk protein as bone tissue engineering scaffolding and the recent application of such silk material as a GBR membrane. We also suggested future studies exploring additional uses of silk-based materials as GBR membranes.

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Li, Xingguo, Bingbing An, and Dongsheng Zhang. "Effect of Interfacial Properties on the Mechanical Behavior of Bone-Like Materials: A Numerical Study." International Journal of Applied Mechanics 09, no. 01 (January 2017): 1750014. http://dx.doi.org/10.1142/s1758825117500144.

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Interfacial behavior in the microstructure and the plastic deformation in the protein matrix influence the overall mechanical properties of biological hard tissues. A cohesive finite element model has been developed to investigate the inelastic mechanical properties of bone-like biocomposites consisting of hard mineral crystals embedded in soft biopolymer matrix. In this study, the complex interaction between plastic dissipation in the matrix and bonding properties of the interface between minerals and matrix is revealed, and the effect of such interaction on the toughening of bone-like biocomposites is identified. For the case of strong and intermediate interfaces, the toughness of biocomposites is controlled by the post yield behavior of biopolymer; the matrix with low strain hardening can undergo significant plastic deformation, thereby promoting enhanced fracture toughness of biocomposites. For the case of weak interfaces, the toughness of biocomposites is governed by the bonding property of the interface, and the post-yield behavior of biopolymer shows negligible effect on the toughness. The findings of this study help to direct the path for designing bioinspired materials with superior mechanical properties.

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Suсhenko, Yuriy, Vladislav Suсhenko, Mikhail Mushtruk, Vladimir Vasyliv, and Yuriy Boyko. "RESEARCH INTO MECHANICAL PROPERTIES OF MINCED MEAT AND FINISHED PRODUCTS." EUREKA: Life Sciences 4 (July 31, 2017): 43–51. http://dx.doi.org/10.21303/2504-5695.2017.00389.

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Studies were conducted of the stressed-strained state of biopolymers of meat, which were exposed to the processes of elastic, residual and highly elastic deformation at cutting and mincing. Analysis of the structure of this natural biopolymer and the evaluation of mechanical characteristics of meat under normal and low temperatures are important factors that are taken into account for the rational selection of meat mincing machines and tools in the production of meat products, minced meat, semi-finished and sausage products. The structure of meat is a system of structured protein fibers, impregnated with tissue fluid, which is protein sol that contains organic and inorganic substances, soluble in it. The tissues that the meat is composed of belong to natural biopolymers, so conducting analytical studies into mechanical properties of meat within the framework of our understanding of the mechanics of polymers will make it possible to improve mincing processes, employed during manufacturing of meat products. In order to prevent meat overheating, the mincing process is performed at several stages. For example, in cutting mechanisms of choppers, they use a row of knives and grids with holes, diameter of which gradually changes from the original size of0.06 mto 0.003-0.002 min the outlet grids. Quality indicators of the finished products are affected by mechanical characteristics of raw materials and the way the cutting process is carried out. In the course of conducted analysis it was found that in modern food production there remain unresolved important problems, which address current issues, related to rheological and structural mechanical properties of meat raw material. First of all, it concerns theoretical and practical developments that enhance an understanding of physico-chemical and mechanical properties of raw materials, which will make it possible to develop theoretical foundations and experimentally substantiate the new conceptual approach to solving the task of improving the quality of semi-finished products and durability of equipment at meat processing enterprises of APC. The research is the basis for constructive and technological solutions, choice of mode, kinematic and dynamic parameters of cutting devices, steel and wear resistant coatings for cutting tools that provide saving of energy and materials at meat mincing, high quality of minced meat. and finished products and appropriate service life of the equipment. It was established that in order to determine characteristics of the strained state of meat, it is necessary to apply a circular diagram of loading-unloading, which allows analysis of behavior of the sample in a closed cycle of changing in external load. An analysis indicates a very large dependence of meat elasticity module on temperature. Dependences of this kind are generally characteristic of polymer bodies.

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MIHU, Georgel, Claudia Veronica UNGUREANU, Vasile BRIA, Marina BUNEA, and Rodica CHIHAI PEȚU. "The Mechanical Properties of Organic Modified Epoxy Resin." Annals of “Dunarea de Jos” University of Galati. Fascicle IX, Metallurgy and Materials Science 43, no. 3 (September 15, 2020): 10–14. http://dx.doi.org/10.35219/mms.2020.3.02.

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Epoxy resins have been presenting a lot of scientific and technical interests and organic modified epoxy resins have recently receiving a great deal of attention. For obtaining the composite materials with good mechanical proprieties, a large variety of organic modification agents were used. For this study gluten and gelatin had been used as modifying agents thinking that their dispersion inside the polymer could increase the polymer biocompatibility. Equal amounts of the proteins were milled together and the obtained compound was used to form 1 to 5% weight ratios organic agents modified epoxy materials. To highlight the effect of these proteins in epoxy matrix mechanical tests as three-point bending and compression were performed.

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Jeevan Prasad Reddy, D., A. Varada Rajulu, V. Arumugam, M. D. Naresh, and M. Muthukrishnan. "Effects of Resorcinol On the Mechanical Properties of Soy Protein Isolate Films." Journal of Plastic Film & Sheeting 25, no. 3-4 (July 2009): 221–33. http://dx.doi.org/10.1177/8756087910365030.

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QIN, ZHAO, STEVEN CRANFORD, THEODOR ACKBAROW, and MARKUS J. BUEHLER. "ROBUSTNESS-STRENGTH PERFORMANCE OF HIERARCHICAL ALPHA-HELICAL PROTEIN FILAMENTS." International Journal of Applied Mechanics 01, no. 01 (March 2009): 85–112. http://dx.doi.org/10.1142/s1758825109000058.

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An abundant trait of biological protein materials are hierarchical nanostructures, ranging through atomistic, molecular to macroscopic scales. By utilizing the recently developed Hierarchical Bell Model, here we show that the use of hierarchical structures leads to an extended physical dimension in the material design space that resolves the conflict between disparate material properties such as strength and robustness, a limitation faced by many synthetic materials. We report materiomics studies in which we combine a large number of alpha-helical elements in all possible hierarchical combinations and measure their performance in the strength-robustness space while keeping the total material use constant. We find that for a large number of constitutive elements, most random structural combinations of elements (> 98%) lead to either high strength or high robustness, reflecting the so-called banana-curve performance in which strength and robustness are mutually exclusive properties. This banana-curve type behavior is common to most engineered materials. In contrast, for few, very specific types of combinations of the elements in hierarchies (< 2%) it is possible to maintain high strength at high robustness levels. This behavior is reminiscent of naturally observed material performance in biological materials, suggesting that the existence of particular hierarchical structures facilitates a fundamental change of the material performance. The results suggest that biological materials may have developed under evolutionary pressure to yield materials with multiple objectives, such as high strength and high robustness, a trait that can be achieved by utilization of hierarchical structures. Our results indicate that both the formation of hierarchies and the assembly of specific hierarchical structures play a crucial role in achieving these mechanical traits. Our findings may enable the development of self-assembled de novo bioinspired nanomaterials based on peptide and protein building blocks.

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Qu, Wanwan, Riina Häkkinen, Jack Allen, Carmine D’Agostino, and Andrew P. Abbott. "Globular and Fibrous Proteins Modified with Deep Eutectic Solvents: Materials for Drug Delivery." Molecules 24, no. 19 (October 4, 2019): 3583. http://dx.doi.org/10.3390/molecules24193583.

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Proteinaceous materials have numerous structures, many of which aid in the roles they perform. Some need to impart strength while others need elasticity or toughness. This study is the first to investigate the modification of both globular and fibrous protein, namely, zein, soy protein and gelatin, using deep eutectic solvents (DES) to form bioplastics, which may have application in drug delivery systems. The effects of DES content on the thermal and mechanical properties of the material were determined. Zein and soy are globular proteins, which both showed a significant change in the properties by the addition of DES. Both of these materials were, however, weaker and less ductile than the starch based materials previously reported in the literature. The material made from gelatin, a fibrous protein, showed variable properties depending on how long they were in contact with each other before pressing. Conductivity and NMR measurements indicate the existence of a continuous liquid phase, which are useful in the demonstrated application of transdermal drug delivery systems. It is shown that pharmaceutical DESs can be gelled with gelatin and this method is three times faster at delivering a pharmaceutical active ingredient across the skin barrier than from a corresponding solid formulation.

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Yu, Zeyang, Yue Ji, Violette Bourg, Mustafa Bilgen, and J. Carson Meredith. "Chitin- and cellulose-based sustainable barrier materials: a review." Emergent Materials 3, no. 6 (December 2020): 919–36. http://dx.doi.org/10.1007/s42247-020-00147-5.

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AbstractThe accumulation of synthetic plastics used in packaging applications in landfills and the environment is a serious problem. This challenge is driving research efforts to develop biodegradable, compostable, or recyclable barrier materials derived from renewable sources. Cellulose, chitin/chitosan, and their combinations are versatile biobased packaging materials because of their diverse biological properties (biocompatibility, biodegradability, antimicrobial properties, antioxidant activity, non-toxicity, and less immunogenic compared to protein), superior physical properties (high surface area, good barrier properties, and mechanical properties), and they can be assembled into different forms and shapes (powders, fibers, films, beads, sponges, gels, and solutions). They can be either assembled into packaging films or used as fillers to improve the properties of other biobased polymers. Methods such as preparation of composites, multilayer coating, and alignment control are used to further improve their barrier, mechanical properties, and ameliorate their moisture sensitivity. With the growing application of cellulose and chitin-based packaging materials, their biodegradability and recyclability are also discussed in this review paper. The future trends of these biobased materials in packaging applications and the possibility of gradually replacing petroleum-based plastics are analyzed in the “Conclusions” section.

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Wei, Yunxiao, Ze’en Huang, Zuolong Yu, Chao Han, and Cairong Yang. "Preparation and Properties of Fractionated Soybean Protein Isolate Films." Materials 14, no. 18 (September 20, 2021): 5436. http://dx.doi.org/10.3390/ma14185436.

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Soybean protein isolate (SPI) and its four fractionated products (7S globulin, 11S globulin, upper soybean residue, and lower soybean residue) were compared by fabricating films and film liquids. The separation and grading effects, rheological properties of the film liquids, and difficulty in uncovering the films, in addition to the mechanical properties, water vapor permeability, oil permeability, and surface morphology of the films, were investigated. Results showed that the centrifugal precipitation method could be used to produce fractionated products. The 7S and 11S globulin films exhibited better hydrogels at lower shear rates than the other SPIs; however, they were more difficult to uncover. The tensile strength of the graded films decreased by varying degrees. However, the elongation at the break of the upper soybean residue film considerably increased, reaching 70.47%. Moreover, the permeability and surface morphology of the film were enhanced or weakened. The fractionated products, 7S and 11S globulin films, exhibited better performance. Overall, this study provides a basis for the improved development and use of fractioned SPI products.

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Fadli, Ahmad, and Iis Sopyan. "Porous ceramics with controllable properties prepared by protein foaming-consolidation method." Journal of Porous Materials 18, no. 2 (March 11, 2010): 195–203. http://dx.doi.org/10.1007/s10934-010-9370-8.

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Tian, M., and R. V. Lewis. "Tubuliform silk protein: A protein with unique molecular characteristics and mechanical properties in the spider silk fibroin family." Applied Physics A 82, no. 2 (November 23, 2005): 265–73. http://dx.doi.org/10.1007/s00339-005-3433-8.

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Wang, S., H. J. Sue, and J. Jane. "Effects of Polyhydric Alcohols on the Mechanical Properties of Soy Protein Plastics." Journal of Macromolecular Science, Part A 33, no. 5 (May 1996): 557–69. http://dx.doi.org/10.1080/10601329608010878.

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HOSOKAWA, Jun, Takashi ENDO, Masashi NISHIYAMA, Takao MORITA, and Muneo FUNAHASHI. "Development of Turtleshell-Work-Materials Using Silk Protein. Thermal and Mechanical Properties of Turtleshell and Hotpressed Fibroin." KOBUNSHI RONBUNSHU 50, no. 12 (1993): 929–34. http://dx.doi.org/10.1295/koron.50.929.

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Ahn, Hyunchul, Da Jeong Gong, Hyun Ho Lee, Joo Yeon Seo, Kyung-Mo Song, Su Jin Eom, and Sang Young Yeo. "Mechanical Properties of Porcine and Fish Skin-Based Collagen and Conjugated Collagen Fibers." Polymers 13, no. 13 (June 29, 2021): 2151. http://dx.doi.org/10.3390/polym13132151.

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Collagen is a protein that is a major component of animal skins and tendons. It is used in various medical, cosmetic, and food products through extraction and purification. The fibrous products of purified collagen fibers extracted from raw mammal materials have relatively excellent mechanical properties and are used for high-end medical products. In this study, we examined collagen materials produced from porcine and fish skins, which are major sources of collagen raw materials. We examined a method for spinning collagen fibers from fish skin-based collagen and analyzed the physical properties of those collagen fibers. In addition, we examined the characteristics and advantages of conjugated fibers according to their porcine- and/or fish skin-based compositions. The spinnability and mechanical properties of these conjugated fibers were analyzed according to their compositions. The mechanical properties of collagen structure are determined by hydroxyproline content and can be manipulated by the composition of collagen in the conjugated fibers.

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Pal, Ramendra K., Nicholas E. Kurland, Subhas C. Kundu, and Vamsi K. Yadavalli. "Fabrication of Silk Microstructures Using Photolithography." MRS Proceedings 1718 (2015): 163–70. http://dx.doi.org/10.1557/opl.2015.437.

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ABSTRACTPrecise spatial patterns and micro and nanostructures of peptides and proteins have widespread applications in tissue engineering, bioelectronics, photonics, and therapeutics. Optical lithography using proteins provides a route to directly fabricate intricate, bio-friendly architectures rapidly and across a range of length scales. The unique mechanical strength, optical properties, biocompatibility and controllable degradation of biomaterials from silkworms offer several advantages in this paradigm. Here, we present the biochemical synthesis and applications of a “protein photoresist” synthesized from the silk proteins, fibroin and sericin. Using light-activated direct-write processes such as photolithography, we show how silk proteins can form high resolution, high fidelity structures in two and three dimensions. Protein features can be precisely patterned at sub-microscale resolution (µm) at the bench-top over macroscale areas (cm), easily and repeatedly with high-throughput. For instance, periodic, microstructured arrays can be patterned over large areas to form structurally induced iridescent patterns and functional opto-electronic structures. We further demonstrate how photocrosslinked protein micro-architectures can function for the spatial guidance of cells without use of cell-adhesive ligands as biocompatible and biodegradable scaffolds. The ease of biochemical functionalization, biocompatibility, as well as favorable mechanical properties and biodegradation of this silk biomaterial provide opportunities for otherwise inaccessible applications as sustainable, bioresorbable protein microdevices.

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Journal articles on the topic 'Mechanical properties of protein materials'

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