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Journal articles on the topic 'Collagen self-assembly'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Cui, Fu-Zhai, Yan Li, and Jun Ge. "Self-assembly of mineralized collagen composites." Materials Science and Engineering: R: Reports 57, no. 1-6 (August 2007): 1–27. http://dx.doi.org/10.1016/j.mser.2007.04.001.

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2

Lisitza, Natalia, Xudong Huang, Hiroto Hatabu, and Samuel Patz. "Exploring collagen self-assembly by NMR." Physical Chemistry Chemical Physics 12, no. 42 (2010): 14169. http://dx.doi.org/10.1039/c0cp00651c.

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3

Saeidi, Nima, Edward A. Sander, and Jeffrey W. Ruberti. "Dynamic shear-influenced collagen self-assembly." Biomaterials 30, no. 34 (December 2009): 6581–92. http://dx.doi.org/10.1016/j.biomaterials.2009.07.070.

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4

Papi, Massimiliano, Valentina Palmieri, Giuseppe Maulucci, Giuseppe Arcovito, Emanuela Greco, Gianluca Quintiliani, Maurizio Fraziano, and Marco De Spirito. "Controlled self assembly of collagen nanoparticle." Journal of Nanoparticle Research 13, no. 11 (March 23, 2011): 6141–47. http://dx.doi.org/10.1007/s11051-011-0327-x.

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5

Huang, Zhao Long, Gui Yang Liu, Ying He, Zhong Zhou Yi, and Jun Ming Guo. "Interaction between Hydroxyapatite and Collagen." Advanced Materials Research 412 (November 2011): 384–87. http://dx.doi.org/10.4028/www.scientific.net/amr.412.384.

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To study the interaction between hydroxyapatite (HAP) and collagen in bone, we researched the phenomenon of collagen biomineralization and self-assembly in viro by uv-vis spectra and circular dichroism (CD) spectra. The materials prepared by self-assembly collagen and collagen-HAP showed layer structures. And the product prepared by collagen-HAP had better and more compact appearance. The decrease of speed of collagen self-assembly was caused by calcium ion or strontium ion added. The trough of CD spectra moved down in calcium-containing solution and moved up when forming precipitation of calcium phosphate from the solution. It indicated that the effect of collagen self-assembly was caused by calcium ions, strontium ions etc. in the solution. The IR spectrum proved that a coordinate bond formed between calcium ion and amide groups on collagen.

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6

Zhang, Ju Cheng, He Ping Yan, Guo Wei Zhang, and Li Zhang. "The Spectrum Properties of Type Ι Collagen Self-Assembly Film." Advanced Materials Research 690-693 (May 2013): 1414–17. http://dx.doi.org/10.4028/www.scientific.net/amr.690-693.1414.

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The type I collagen was used to prepare self-assembly film, the UV-vis spectrophotometer and Fluorescence spectrophotometer were employed to characterize those self-assembly films. The Fe (NO3)3 and CuSO4 were used as the additive to investigate the effect of the type I collagen film. It was found that the character spectra of collagen solution and self-assembly film were different, the Fe (NO3)3 enhanced the 408nm fluorescence emission peak, and CuSO4 caused a new emission peak at 399nm. The changes in the fluorescence of films suggest that the metal salt could affect the type I collagen self-assembly.

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7

Kotch, F. W., and R. T. Raines. "Self-assembly of synthetic collagen triple helices." Proceedings of the National Academy of Sciences 103, no. 9 (February 17, 2006): 3028–33. http://dx.doi.org/10.1073/pnas.0508783103.

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8

Gore, Tushar, Yoav Dori, Yeshayahu Talmon, Matthew Tirrell, and Havazelet Bianco-Peled. "Self-Assembly of Model Collagen Peptide Amphiphiles." Langmuir 17, no. 17 (August 2001): 5352–60. http://dx.doi.org/10.1021/la010223i.

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9

NOITUP, PAWEENA, MICHAEL T. MORRISSEY, and WUNWIBOON GARNJANAGOONCHORN. "IN VITRO SELF-ASSEMBLY OF SILVER-LINE GRUNT TYPE I COLLAGEN: EFFECTS OF COLLAGEN CONCENTRATIONS, pH AND TEMPERATURES ON COLLAGEN SELF-ASSEMBLY." Journal of Food Biochemistry 30, no. 5 (October 2006): 547–55. http://dx.doi.org/10.1111/j.1745-4514.2006.00081.x.

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10

Yurchenco, P. D., E. C. Tsilibary, A. S. Charonis, and H. Furthmayr. "Models for the self-assembly of basement membrane." Journal of Histochemistry & Cytochemistry 34, no. 1 (January 1986): 93–102. http://dx.doi.org/10.1177/34.1.3510247.

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Basement membranes contain a number of intrinsic macromolecular components which are unique to these structures and which cooperatively assemble into specific heteropolymeric matrices. Type IV collagen triple helical monomers bind together at their amino-terminal, carboxy-terminal, and lateral domains to form a lattice-like array. Laminin, in a two-step process, binds to itself at its terminal globular domains to form polymers and also binds collagen at two distinct sites along the collagen chain. Heparan sulfate proteoglycan has been found to bind both collagen and laminin, suggesting a reversible crosslinking function. On the basis of the data derived from self-association studies, it is possible to begin considering models for the assembly and structure of these ubiquitous matrices.

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11

Song, Xuan, Zhiwei Wang, Shiyu Tao, Guixia Li, and Jie Zhu. "Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy." Journal of Food Quality 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/9257060.

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Self-assembly of extracted collagen from swine trotter tendon under different conditions was firstly observed using atomic force microscopy; then the effects of collagen concentration, pH value, and metal ions to the topography of the collagen assembly were analyzed with the height images and section analysis data. Collagen assembly under 0.1 M, 0.2 M, 0.3 M CaCl2, and MgCl2 solutions in different pH values showed significant differences (P < 0.05) in the topographical properties including height, width, and roughness. With the concentration being increased, the width of collagen decreased significantly (P < 0.05). The width of collagen fibers was first increased significantly (P < 0.05) and then decreased with the increasing of pH. The collagen was assembled with network structure on the mica in solution with Ca2+ ions. However, it had shown uniformed fibrous structure with Mg2+ ions on the new cleaved mica sheet. In addition, the width of collagen fibrous was 31~58 nm in solution with Mg2+ but 21~50 nm in Ca2+ solution. The self-assembly collagen displayed various potential abilities to construct fibers or membrane on mica surfaces with Ca2+ ions and Mg2+ irons. Besides, the result of collagen self-assembly had shown more relations among solution pH value, metal ions, and collagen molecular concentration, which will provide useful information on the control of collagen self-assembly in tissue engineering and food packaging engineering.

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12

Strasser, Stefan, Albert Zink, Wolfgang M. Heckl, and Stefan Thalhammer. "Controlled Self-Assembly of Collagen Fibrils by an Automated Dialysis System." Journal of Biomechanical Engineering 128, no. 5 (March 12, 2006): 792–96. http://dx.doi.org/10.1115/1.2264392.

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In vitro self-assembled collagen fibrils form a variety of different structures during dialysis. The self-assembly is dependent on several parameters, such as concentrations of collagen and α1-acid glycoprotein, temperature, dialysis time, and the acid concentration. For a detailed understanding of the assembly pathway and structural features like banding pattern or mechanical properties it is necessary to study single collagen fibrils. In this work we present a fully automated system to control the permeation of molecules through a membrane like a dialysis tubing. This allows us to ramp arbitrary diffusion rate profiles during the self-assembly process of macromolecules, such as collagen. The system combines a molecular sieving method with a computer assisted control system for measuring process variables. With the regulation of the diffusion rate it is possible to control and manipulate the collagen self-assembly process during the whole process time. Its performance is demonstrated by the preparation of various collagen type I fibrils and native collagen type II fibrils. The combination with the atomic force microscope (AFM) allows a high resolution characterization of the self-assembled fibrils. In principle, the represented system can be also applied for the production of other biomolecules, where a dialysis enhanced self-assembly process is used.

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13

Reimer, Armando E., Katie M. Feher, Daniel Hernandez, and Katarzyna Slowinska. "Self-assembly of collagen peptides into hollow microtubules." Journal of Materials Chemistry 22, no. 16 (2012): 7701. http://dx.doi.org/10.1039/c2jm16122b.

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14

Salhi, Billel, François Vaurette, Bruno Grandidier, Didier Stiévenard, Oleg Melnyk, Yannick Coffinier, and Rabah Boukherroub. "The collagen assisted self-assembly of silicon nanowires." Nanotechnology 20, no. 23 (May 19, 2009): 235601. http://dx.doi.org/10.1088/0957-4484/20/23/235601.

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15

Hasan, Nida F., Avanish S. Parmar, Mihir Joshi, Patrick Nosker, and Vikas Nanda. "Charge Crowding Promotes Self-Assembly of Collagen Hetrotrimers." Biophysical Journal 106, no. 2 (January 2014): 680a—681a. http://dx.doi.org/10.1016/j.bpj.2013.11.3768.

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16

Narayanan, Badri, George H. Gilmer, Jinhui Tao, James J. De Yoreo, and Cristian V. Ciobanu. "Self-Assembly of Collagen on Flat Surfaces: The Interplay of Collagen–Collagen and Collagen–Substrate Interactions." Langmuir 30, no. 5 (January 28, 2014): 1343–50. http://dx.doi.org/10.1021/la4043364.

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17

Wang, Zhiwei, Qi Xiao, Xuan Song, Yunfei Wan, and Jie Zhu. "Cation-Specific Effects on the Self-Assembly of Collagen Molecules Mediated by Acetate on Mica Surface Observed with Atomic Force Microscopy." Journal of Food Quality 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/1692975.

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The well-organized collagen layers on mica surface have drawn extensive attention for its essential applications and studies on the process of self-assembly as a model system. In this work, collagen extracted from fish scales by acid-base method was used to explore the self-assembly characters, and atomic force microscopy was applied to observe the collagen assembled on mica surface mediated by acetate with four different cations, including K+, Na+, Mg2+, and Ca2+. It showed that cations might influence the interaction between collagen fibrils and mica surface at high ionic concentration. And a similar network structure was acquired with uniform pore size for four kinds of acetates; nearly ranged collagen fibrils in the same direction were collected in Mg2+ solutions, while flat films with some fibrils were achieved in K+ solutions. The Hofmeister series and Collins’ model were adapted to explain the effects of cations and acetate on the self-assembly of collagen. These results and analysis would be helpful for directing the pattern of collagen assembly on a solid surface with a potential application in food science and engineering.

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18

Norris, Karl, Oksana Mishukova, Agata Zykwinska, Sylvia Colliec-Jouault, Corinne Sinquin, Andrei Koptioug, Stéphane Cuenot, et al. "Marine Polysaccharide-Collagen Coatings on Ti6Al4V Alloy Formed by Self-Assembly." Micromachines 10, no. 1 (January 19, 2019): 68. http://dx.doi.org/10.3390/mi10010068.

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Polysaccharides of marine origin are gaining interest as biomaterial components. Bacteria derived from deep-sea hydrothermal vents can produce sulfated exopolysaccharides (EPS), which can influence cell behavior. The use of such polysaccharides as components of organic, collagen fibril-based coatings on biomaterial surfaces remains unexplored. In this study, collagen fibril coatings enriched with HE800 and GY785 EPS derivatives were deposited on titanium alloy (Ti6Al4V) scaffolds produced by rapid prototyping and subjected to physicochemical and cell biological characterization. Coatings were formed by a self-assembly process whereby polysaccharides were added to acidic collagen molecule solution, followed by neutralization to induced self-assembly of collagen fibrils. Fibril formation resulted in collagen hydrogel formation. Hydrogels formed directly on Ti6Al4V surfaces, and fibrils adsorbed onto the surface. Scanning electron microscopy (SEM) analysis of collagen fibril coatings revealed association of polysaccharides with fibrils. Cell biological characterization revealed good cell adhesion and growth on bare Ti6Al4V surfaces, as well as coatings of collagen fibrils only and collagen fibrils enhanced with HE800 and GY785 EPS derivatives. Hence, the use of both EPS derivatives as coating components is feasible. Further work should focus on cell differentiation.

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19

Puttawibul, Puttiporn, Soottawat Benjakul, and Jirut Meesane. "Freeze-Thawed Hybridized Preparation with Biomimetic Self-Assembly for a Polyvinyl Alcohol/Collagen Hydrogel Created for Meniscus Tissue Engineering." Journal of Biomimetics, Biomaterials and Biomedical Engineering 21 (August 2014): 17–33. http://dx.doi.org/10.4028/www.scientific.net/jbbbe.21.17.

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Freeze-thawed hybridized preparation and the biomimetic self-assembly technique were used to fabricate hydrogel as tissue engineered scaffolds for meniscus tissue. Because of the advantages of both techniques, they were hybridized together as an interesting preparation for hydrogel. Three molecular weights (high, medium, and low) of PVA were prepared in a biomimetic solution before formation into hydrogel by freeze-thawing. The most suitable molecular weight PVA for hydrogel formation was chosen to be mixed with collagen. PVA, PVA/collagen, and collagen were prepared in biomimetic solutions and freeze-thawed into hydrogels. The hydrogels were analyzed and characterized by FTIR, DSC, and SEM. FTIR characterization indicated that high molecular weight PVA formed molecular interaction better than the other molecular weights, and PVA molecules formed molecular interaction with collagen molecules via –OH and C=O groups. DSC characterization showed that the hybridized preparation of freeze-thawing and biomimetic self-assembly kept the characteristics of PVA and collagen. SEM analysis demonstrated that the morphological formation of PVA/collagen was hybridized during freeze-thawing and collagen self-assembly. The morphological structure was organized into a porous network structure. The porous structure showed a rough wall that was formed by the hybridized structure of the crystal domain dispersed in amorphous and collagen self-assembly.

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20

Zhu, Weizhe, Ke Li, Qi Liu, Huaying Zhong, Chengzhi Xu, Juntao Zhang, Huizhi Kou, Benmei Wei, and Haibo Wang. "Effect of molecular chirality on the collagen self-assembly." New Journal of Chemistry 45, no. 35 (2021): 15863–68. http://dx.doi.org/10.1039/d1nj02242c.

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21

Hu, Changmin, Le Yu, and Mei Wei. "Biomimetic intrafibrillar silicification of collagen fibrils through a one-step collagen self-assembly/silicification approach." RSC Advances 7, no. 55 (2017): 34624–32. http://dx.doi.org/10.1039/c7ra02935g.

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22

Zhang, W., S. S. Liao, and F. Z. Cui. "Hierarchical Self-Assembly of Nano-Fibrils in Mineralized Collagen." Chemistry of Materials 15, no. 16 (August 2003): 3221–26. http://dx.doi.org/10.1021/cm030080g.

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23

Köster, Sarah, Heather M. Evans, Joyce Y. Wong, and Thomas Pfohl. "An In Situ Study of Collagen Self-Assembly Processes." Biomacromolecules 9, no. 1 (January 2008): 199–207. http://dx.doi.org/10.1021/bm700973t.

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24

Przybyla, David E., and Jean Chmielewski. "Metal-Triggered Radial Self-Assembly of Collagen Peptide Fibers." Journal of the American Chemical Society 130, no. 38 (September 24, 2008): 12610–11. http://dx.doi.org/10.1021/ja804942w.

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25

Ludwig, Nicholas S., Colin Yoder, Michael McConney, Terrence G. Vargo, and Khalid N. Kader. "Directed type IV collagen self-assembly on hydroxylated PTFE." Journal of Biomedical Materials Research Part A 78A, no. 3 (2006): 615–19. http://dx.doi.org/10.1002/jbm.a.30776.

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26

Pidaparti, Ramana M., Karthik Murugesan, and Hiroki Yokota. "Computational Framework for Nanoscale Self-Assembly of Collagen Fiber." Journal of Computational and Theoretical Nanoscience 3, no. 5 (October 1, 2006): 643–48. http://dx.doi.org/10.1166/jctn.2006.004.

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27

Pidaparti, Ramana M., Karthik Murugesan, and Hiroki Yokota. "Computational Framework for Nanoscale Self-Assembly of Collagen Fiber." Journal of Computational and Theoretical Nanoscience 3, no. 5 (October 1, 2006): 643–48. http://dx.doi.org/10.1166/jctn.2006.3048.

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28

Shayegan, Marjan, Tuba Altindal, and Nancy R. Forde. "Investigating the Mechanism of Collagen Self-Assembly with Microrheology." Biophysical Journal 106, no. 2 (January 2014): 55a. http://dx.doi.org/10.1016/j.bpj.2013.11.386.

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29

Kunii, Saori, Michiko Shibano, Takuya Saito, and Koichi Morimoto. "1P189 Thermal stability and structural feature of actinidain-hydrolyzed collagen self-assembly(6. Macromolecular assembly,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)." Seibutsu Butsuri 46, supplement2 (2006): S194. http://dx.doi.org/10.2142/biophys.46.s194_1.

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30

Nair, Malavika, Yonatan Calahorra, Sohini Kar-Narayan, Serena M. Best, and Ruth E. Cameron. "Self-assembly of collagen bundles and enhanced piezoelectricity induced by chemical crosslinking." Nanoscale 11, no. 32 (2019): 15120–30. http://dx.doi.org/10.1039/c9nr04750f.

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The choice of crosslinking is shown to enhance the piezoelectric response of a collagen construct. In particular, EDC-NHS crosslinking induces the self-assembly of collagen bundles which present a localised piezoelectric response.

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31

Banerjee, Jayati, and Helena S. Azevedo. "Crafting of functional biomaterials by directed molecular self-assembly of triple helical peptide building blocks." Interface Focus 7, no. 6 (October 20, 2017): 20160138. http://dx.doi.org/10.1098/rsfs.2016.0138.

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Collagen is the most abundant extracellular matrix protein in the body and has widespread use in biomedical research, as well as in clinics. In addition to difficulties in the production of recombinant collagen due to its high non-natural imino acid content, animal-derived collagen imposes several major drawbacks—variability in composition, immunogenicity, pathogenicity and difficulty in sequence modification—that may limit its use in the practical scenario. However, in recent years, scientists have shifted their attention towards developing synthetic collagen-like materials from simple collagen model triple helical peptides to eliminate the potential drawbacks. For this purpose, it is highly desirable to develop programmable self-assembling strategies that will initiate the hierarchical self-assembly of short peptides into large-scale macromolecular assemblies with recommendable bioactivity. Herein, we tried to elaborate our understanding related to the strategies that have been adopted by few research groups to trigger self-assembly in the triple helical peptide system producing fascinating supramolecular structures. We have also touched upon the major epitopes within collagen that can be incorporated into collagen mimetic peptides for promoting bioactivity.

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32

Silver, Frederick H., Joseph W. Freeman, and Gurinder P. Seehra. "Collagen self-assembly and the development of tendon mechanical properties." Journal of Biomechanics 36, no. 10 (October 2003): 1529–53. http://dx.doi.org/10.1016/s0021-9290(03)00135-0.

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33

Evans, G. T. "Molecular self assembly of rodlike particles: An application to collagen." Journal of Chemical Physics 109, no. 6 (August 8, 1998): 2519–27. http://dx.doi.org/10.1063/1.476824.

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34

Luo, Jingnan, and Yen Wah Tong. "Self-Assembly of Collagen-Mimetic Peptide Amphiphiles into Biofunctional Nanofiber." ACS Nano 5, no. 10 (September 14, 2011): 7739–47. http://dx.doi.org/10.1021/nn202822f.

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35

de la Rica, Roberto, Ernest Mendoza, Lesley W. Chow, Kristy L. Cloyd, Sergio Bertazzo, Hannah C. Watkins, Joseph A. M. Steele, and Molly M. Stevens. "Self-Assembly of Collagen Building Blocks Guided by Electric Fields." Small 10, no. 19 (June 10, 2014): 3876–79. http://dx.doi.org/10.1002/smll.201400424.

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36

Gayatri, Raghuraman, Ashok Kumar Sharma, Rama Rajaram, and Thirumalachari Ramasami. "Chromium(III)-Induced Structural Changes and Self-Assembly of Collagen." Biochemical and Biophysical Research Communications 283, no. 1 (April 2001): 229–35. http://dx.doi.org/10.1006/bbrc.2001.4713.

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37

Pires, Marcos M., and Jean Chmielewski. "Self-assembly of Collagen Peptides into Microflorettes via Metal Coordination." Journal of the American Chemical Society 131, no. 7 (February 25, 2009): 2706–12. http://dx.doi.org/10.1021/ja8088845.

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38

Tsilibary, E. C., and A. S. Charonis. "The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly." Journal of Cell Biology 103, no. 6 (December 1, 1986): 2467–73. http://dx.doi.org/10.1083/jcb.103.6.2467.

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Type IV collagen incubated at elevated temperatures in physiologic buffers self-associates (a) via its carboxy-terminal (NC1) domain, (b) via its amino-terminal (7S) domain, and (c) laterally; and it forms a network. When examined with the technique of rotary shadowing, isolated domain NC1 was found to bind along the length of type IV collagen to four distinct sites located at intervals of approximately 100 nm each. The same 100-nm distance was observed in domain NC1 of intact type IV collagen bound along the length of the collagen molecules during initial steps of network formation and in complete networks. The presence of anti-NC1 Fab fragments in type IV collagen solutions inhibited lateral association and network formation in rotary shadow images. During the process of self-association type IV collagen develops turbidity; addition of isolated domain NC1 inhibited the development of turbidity in a concentration-dependent manner. These findings indicate that domain NC1 of type IV collagen plays an important role in the process of self-association and suggest that alterations in the structure of NC1 may be partially responsible for impaired functions of basement membranes in certain pathological conditions.

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39

Lin, Mingli, Huanhuan Liu, Jingjing Deng, Ran An, Minjuan Shen, Yanqiu Li, and Xu Zhang. "Carboxymethyl chitosan as a polyampholyte mediating intrafibrillar mineralization of collagen via collagen/ACP self-assembly." Journal of Materials Science & Technology 35, no. 9 (September 2019): 1894–905. http://dx.doi.org/10.1016/j.jmst.2019.05.010.

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40

Tsilibary, E. C., G. G. Koliakos, A. S. Charonis, A. M. Vogel, L. A. Reger, and L. T. Furcht. "Heparin type IV collagen interactions: equilibrium binding and inhibition of type IV collagen self-assembly." Journal of Biological Chemistry 263, no. 35 (December 1988): 19112–18. http://dx.doi.org/10.1016/s0021-9258(18)37397-6.

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41

Zhong, Huaying, Weizhe Zhu, Zihan Yan, Chengzhi Xu, Benmei Wei, and Haibo Wang. "A quantum dot-based fluorescence sensing platform for the efficient and sensitive monitoring of collagen self-assembly." New Journal of Chemistry 44, no. 26 (2020): 11304–9. http://dx.doi.org/10.1039/d0nj01346c.

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42

He, Lan, Wang, Ahmed, and Liu. "Extraction and Characterization of Self-Assembled Collagen Isolated from Grass Carp and Crucian Carp." Foods 8, no. 9 (September 6, 2019): 396. http://dx.doi.org/10.3390/foods8090396.

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Collagens were extracted from grass carp skin (GCC), grass carp scales (GSC), and crucian carp skin (CCC) using an acid-enzyme combination method, and their characteristics and self-assembly properties were analyzed. Electrophoretic patterns characterized all three as type I collagens. An ultraviolet analysis identified the optimal wavelengths for collagen detection, while a Fourier transform infrared spectroscopy analysis confirmed the triple-helical structure of the collagens. The GCC, GSC, and CCC had denaturation temperatures of 39.75, 34.49, and 39.05 °C, respectively. All three were shown to self-assemble into fibrils at 30 °C in the presence of NaCl, but the fibril formation rate of CCC (40%) was slightly higher than those of GCC (28%) and GSC (27%). The GSC were shown to form a more strongly intertwined fibril network with a characteristic D-periodicity. The fish collagens extracted in this study have potential applications in the development of functionalized materials.

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43

Okamoto, Mitsuyo, E. Iwai, H. Hatta, Hitoshi Kohri, and Ichiro Shiota. "New Fabrication Process of Nano–Composites by Biomimetic Approach." Advances in Science and Technology 58 (September 2008): 60–65. http://dx.doi.org/10.4028/www.scientific.net/ast.58.60.

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In bio-systems, nano-composites with complex micro-structures are formed by self-assembly only using low energy at room temperature. If these mechanisms of biological tissue are identified, we can possibly propose a new process to fabricate composites by mimicking tissue formation in vivo. As a bio-material, we paid attention to bio-tissue reinforced with collagen fibrils. Collagen fibrils are of baculiform; Thus the self-assembly process through liquid crystalline transition has been proposed by a French group [1]. In the present study, factors controlling liquid crystalline transition, e.g. concentration and pH, are discussed using collagen solution. When liquid crystalline phase is produced, aligned molecules exhibits optical anisotropy. This anisotropy was observed with a polarized optical microscopy (POM). By observations with POM, development of cholesteric phase in collagen solution was clarified.

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44

Zheng, Hongning, Cheng Lu, Jun Lan, Shilong Fan, Vikas Nanda, and Fei Xu. "How electrostatic networks modulate specificity and stability of collagen." Proceedings of the National Academy of Sciences 115, no. 24 (May 29, 2018): 6207–12. http://dx.doi.org/10.1073/pnas.1802171115.

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One-quarter of the 28 types of natural collagen exist as heterotrimers. The oligomerization state of collagen affects the structure and mechanics of the extracellular matrix, providing essential cues to modulate biological and pathological processes. A lack of high-resolution structural information limits our mechanistic understanding of collagen heterospecific self-assembly. Here, the 1.77-Å resolution structure of a synthetic heterotrimer demonstrates the balance of intermolecular electrostatics and hydrogen bonding that affects collagen stability and heterospecificity of assembly. Atomistic simulations and mutagenesis based on the solved structure are used to explore the contributions of specific interactions to energetics. A predictive model of collagen stability and specificity is developed for engineering novel collagen structures.

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45

Mcbride, jr., Daniel J., Karl E. Kadler, Yoshio Hojima, and Darwin J. Prockop. "Self-Assembly into Fibrils of a Homotrimer of Type I Collagen." Matrix 12, no. 4 (August 1992): 256–63. http://dx.doi.org/10.1016/s0934-8832(11)80077-6.

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46

Zhu, Shichen, Qijuan Yuan, Tao Yin, Juan You, Zhipeng Gu, Shanbai Xiong, and Yang Hu. "Self-assembly of collagen-based biomaterials: preparation, characterizations and biomedical applications." Journal of Materials Chemistry B 6, no. 18 (2018): 2650–76. http://dx.doi.org/10.1039/c7tb02999c.

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Xu, Peng, Jia Huang, Peggy Cebe, and David L. Kaplan. "Osteogenesis Imperfecta Collagen-Like Peptides: Self-Assembly and Mineralization on Surfaces." Biomacromolecules 9, no. 6 (June 2008): 1551–57. http://dx.doi.org/10.1021/bm701365x.

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Choi, Jae-Won, Jong-Woo Kim, In-Hwan Jo, Young-Hag Koh, and Hyoun-Ee Kim. "Novel Self-Assembly-Induced Gelation for Nanofibrous Collagen/Hydroxyapatite Composite Microspheres." Materials 10, no. 10 (September 21, 2017): 1110. http://dx.doi.org/10.3390/ma10101110.

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Fang, Ming, Elizabeth L. Goldstein, Eryn K. Matich, Bradford G. Orr, and Mark M. Banaszak Holl. "Type I Collagen Self-Assembly: The Roles of Substrate and Concentration." Langmuir 29, no. 7 (February 7, 2013): 2330–38. http://dx.doi.org/10.1021/la3048104.

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Jiang, Tao, Chunfu Xu, Yang Liu, Zheng Liu, Joseph S. Wall, Xiaobing Zuo, Tianquan Lian, et al. "Structurally Defined Nanoscale Sheets from Self-Assembly of Collagen-Mimetic Peptides." Journal of the American Chemical Society 136, no. 11 (March 10, 2014): 4300–4308. http://dx.doi.org/10.1021/ja412867z.

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