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Relevant bibliographies by topics / Polypeptides. Peptides

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Academic literature on the topic 'Polypeptides. Peptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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Journal articles on the topic "Polypeptides. Peptides"

1

McQuaid, Conor, Andrea Halsey, Maëva Dubois, Ignacio Romero, and David Male. "Comparison of polypeptides that bind the transferrin receptor for targeting gold nanocarriers." PLOS ONE 16, no. 6 (June 4, 2021): e0252341. http://dx.doi.org/10.1371/journal.pone.0252341.

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The ability to target therapeutic agents to specific tissues is an important element in the development of new disease treatments. The transferrin receptor (TfR) is one potential target for drug delivery, as it expressed on many dividing cells and on brain endothelium, the key cellular component of the blood-brain barrier. The aim of this study was to compare a set of new and previously-described polypeptides for their ability to bind to brain endothelium, and investigate their potential for targeting therapeutic agents to the CNS. Six polypeptides were ranked for their rate of endocytosis by the human brain endothelial cell line hCMEC/D3 and the murine line bEnd.3. One linear polypeptide and two cyclic polypeptides showed high rates of uptake. These peptides were investigated to determine whether serum components, including transferrin itself affected uptake by the endothelium. One of the cyclic peptides was strongly inhibited by transferrin and the other cyclic peptide weakly inhibited. As proof of principle the linear peptide was attached to 2nm glucose coated gold-nanoparticles, and the rate of uptake of the nanoparticles measured in a hydrogel model of the blood-brain barrier. Attachment of the TfR-targeting polypeptide significantly increased the rates of endocytosis by brain endothelium and increased movement of nanoparticles across the cells.

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Evans, John Spencer, Ram Samudrala, Tiffany R. Walsh, Ersin Emre Oren, and Candan Tamerler. "Molecular Design of Inorganic-Binding Polypeptides." MRS Bulletin 33, no. 5 (May 2008): 514–18. http://dx.doi.org/10.1557/mrs2008.103.

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AbstractControlled binding and assembly of peptides onto inorganic substrates is at the core of bionanotechnology and biological-materials engineering. Peptides offer several unique advantages for developing future inorganic materials and systems. First, engineered polypeptides can molecularly recognize inorganic surfaces that are distinguishable by shape, crystallography, mineralogy, and chemistry. Second, polypeptides are capable of self-assembly on specific material surfaces leading to addressable molecular architectures. Finally, genetically engineered peptides offer multiple strategies for their functional modification. In this article, we summarize the details and mechanisms involved in combinatorial-polypeptide sequence selection and inorganic-material recognition and affinity, and outline experimental and theoretical approaches and concepts that will help advance this emerging field.

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Ibeanu, Nkiruka, Raphael Egbu, Lesley Onyekuru, Hoda Javaheri, Peng Tee Khaw, Gareth R. Williams, Steve Brocchini, and Sahar Awwad. "Injectables and Depots to Prolong Drug Action of Proteins and Peptides." Pharmaceutics 12, no. 10 (October 21, 2020): 999. http://dx.doi.org/10.3390/pharmaceutics12100999.

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Proteins and peptides have emerged in recent years to treat a wide range of multifaceted diseases such as cancer, diabetes and inflammation. The emergence of polypeptides has yielded advancements in the fields of biopharmaceutical production and formulation. Polypeptides often display poor pharmacokinetics, limited permeability across biological barriers, suboptimal biodistribution, and some proclivity for immunogenicity. Frequent administration of polypeptides is generally required to maintain adequate therapeutic levels, which can limit efficacy and compliance while increasing adverse reactions. Many strategies to increase the duration of action of therapeutic polypeptides have been described with many clinical products having been developed. This review describes approaches to optimise polypeptide delivery organised by the commonly used routes of administration. Future innovations in formulation may hold the key to the continued successful development of proteins and peptides with optimal clinical properties.

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Skelton, Nicholas J., Tamas Blandl, Stephen J. Russell, Melissa A. Starovasnik, and Andrea G. Cochran. "β‒hairpin polypeptides by design and selection." Spectroscopy 17, no. 2-3 (2003): 213–30. http://dx.doi.org/10.1155/2003/148024.

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We have developed polypeptide scaffolds that readily adopt aβ‒hairpin conformation (a pair of antiparallel strands connected by a turn) in solution. The study of such peptides allows us to understand the factors that govern stability and folding of these motifs in proteins, and permits mimicry of functionally important regions of proteins. Spectroscopic and biophysical methods have been used to characterize the conformational preferences and stability of these peptides, with a strong emphasis on using restraints generated from1H NMR spectroscopy to determine their three‒dimensional structure. By optimization of inter‒strand interactions, we have developed highly stable disulfide‒cyclized and linearβ‒hairpin peptides. In particular, tryptophan residues at non‒hydrogen bonded strand sites (NHB) are highly stabilizing. A variety of turn types have been presented from these scaffolds, suggesting that they might generally be useful in turn presentation. Interestingly,β‒hairpin peptides (containing a disulfide and a NHB tryptophan) have recently been discovered as antagonists of protein–protein interactions from naïve peptide libraries displayed on phage. Comparison of one suchβ‒hairpin peptide with anα‒helical peptide of very similar sequence provides further insight into the role that residue type and context play in determining polypeptide conformation.

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Fidelio, G. D., B. M. Austen, D. Chapman, and J. A. Lucy. "Properties of signal-sequence peptides at an air-water interface." Biochemical Journal 238, no. 1 (August 15, 1986): 301–4. http://dx.doi.org/10.1042/bj2380301.

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The surface behaviour of three signal-sequence polypeptides (the pretrypsinogen 2 signal sequence, a synthetic consensus signal sequence and the putative signal sequence of ovalbumin) were studied at an air-water interface. It was found that the surface stabilities of the spread polypeptide films were higher than those of polypeptides and proteins previously investigated (including melittin and membrane proteins), and that the signal peptides had a much lower affinity for the interface than had other peptides and proteins. The observed molecular areas of the signal-sequence peptides indicated that the molecules have a considerable degree of secondary structure at the surface interface.

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Xiong, Menghua, Michelle W. Lee, Rachael A. Mansbach, Ziyuan Song, Yan Bao, Richard M. Peek, Catherine Yao, et al. "Helical antimicrobial polypeptides with radial amphiphilicity." Proceedings of the National Academy of Sciences 112, no. 43 (October 12, 2015): 13155–60. http://dx.doi.org/10.1073/pnas.1507893112.

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α-Helical antimicrobial peptides (AMPs) generally have facially amphiphilic structures that may lead to undesired peptide interactions with blood proteins and self-aggregation due to exposed hydrophobic surfaces. Here we report the design of a class of cationic, helical homo-polypeptide antimicrobials with a hydrophobic internal helical core and a charged exterior shell, possessing unprecedented radial amphiphilicity. The radially amphiphilic structure enables the polypeptide to bind effectively to the negatively charged bacterial surface and exhibit high antimicrobial activity against both gram-positive and gram-negative bacteria. Moreover, the shielding of the hydrophobic core by the charged exterior shell decreases nonspecific interactions with eukaryotic cells, as evidenced by low hemolytic activity, and protects the polypeptide backbone from proteolytic degradation. The radially amphiphilic polypeptides can also be used as effective adjuvants, allowing improved permeation of commercial antibiotics in bacteria and enhanced antimicrobial activity by one to two orders of magnitude. Designing AMPs bearing this unprecedented, unique radially amphiphilic structure represents an alternative direction of AMP development; radially amphiphilic polypeptides may become a general platform for developing AMPs to treat drug-resistant bacteria.

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Chatterjee, Sunanda, Rituparna Sinha Roy, and P. Balaram. "Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of α-amino acids." Journal of The Royal Society Interface 4, no. 15 (January 23, 2007): 587–606. http://dx.doi.org/10.1098/rsif.2006.0203.

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Half a century has passed since the hydrogen-bonded secondary structures of polypeptides and proteins were first recognized. An extraordinary wealth of conformational information is now available on peptides and proteins, which are formed of α-amino acid residues. More recently, the discovery of well-folded structures in oligopeptides containing β-amino acids has focused a great deal of current interest on the conformational properties of peptides constructed from higher homologues (ω) of α-amino acids. This review examines the nature of intramolecularly hydrogen-bonded conformations of hybrid peptides formed by amino acid residues, with a varying number of backbone atoms. The β-turn, a ubiquitous structural feature formed by two residue (αα) segments in proteins and peptides, is stabilized by a 10-atom (C 10 ) intramolecular 4→1 hydrogen bond. Hybrid turns may be classified by comparison with their αα counterparts. The available crystallographic information on hydrogen-bonded hybrid turns is surveyed in this review. Several recent examples demonstrate that individual ω-amino acid residues and hybrid dipeptide segments may be incorporated into the regular structures of α-peptides. Examples of both peptide helices and hairpins are presented. The present review explores the relationships between folded conformations in hybrid sequences and their counterparts in all α-residue sequences. The use of stereochemically constrained ω-residues promises to expand the range of peptide design strategies to include ω-amino acids. This approach is exemplified by well-folded structures like the C 12 (αγ) and C 14 (γγ) helices formed in short peptides containing multiply substituted γ-residues. The achiral γ-residue gabapentin is a readily accessible building block in the design of peptides containing γ-amino acids. The construction of globular polypeptide structures using diverse hybrid sequences appears to be a realistic possibility.

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Nan, Nan, and Xi Jing Liu. "Study on Degradation of Radix Isatidis Polypeptide in Artificial Gastrointestinal Environment." Advanced Materials Research 989-994 (July 2014): 1020–24. http://dx.doi.org/10.4028/www.scientific.net/amr.989-994.1020.

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Radix Isatidis is a traditional Chinese medicine for treatment of influenza and inflammation in China. In this paper, in order to study the degradation situation of Radix Isatidis polypeptide in artificial gastrointestinal environment, the SDS-PAGE (Sodium dodecyl sulfate-polyacrylamide gel electrophoresis) method was used to detect the degradation of Radix Isatidis polypeptide in artificial intestinal juice and gastric juice, and it showed that Radix Isatidis peptides could be degradated to different degrees. HPLC (High Performance Liquid Chromatography) was used to determine the change of peptides degradation, and it indicated that free amino acid levels did not change significantly. The result after degradation was also detected by BCA method, and it showed that there were still a large number of polypeptides in the liquid. From this experiment we can come to this conclusion that Radix Isatidis polypeptides in artificial gastrointestinal juice mostly degraded into a series of different molecular weight peptides.

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Cole, D. G., W. Z. Cande, R. J. Baskin, D. A. Skoufias, C. J. Hogan, and J. M. Scholey. "Isolation of a sea urchin egg kinesin-related protein using peptide antibodies." Journal of Cell Science 101, no. 2 (February 1, 1992): 291–301. http://dx.doi.org/10.1242/jcs.101.2.291.

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To understand the roles of kinesin and its relatives in cell division, it is necessary to identify and characterize multiple members of the kinesin superfamily from mitotic cells. To this end we have raised antisera to peptides corresponding to highly conserved regions of the motor domains of several known members of the kinesin superfamily. These peptide antibodies react specifically with the motor domains of kinesin and ncd protein, as expected, and they also react with several polypeptides (including kinesin heavy chain) that cosediment with microtubules (MTs) precipitated from AMPPNP-treated sea urchin egg cytosol. Subsequent fractionation of ATP eluates of these MTs yields a protein of relative molecular mass 330 × 10(3) that behaves as a complex of three polypeptides that are distinct from conventional kinesin subunits or fragments thereof. This complex contains 85 kDa and 95 kDa polypeptides, which react with our peptide antibodies, and a 115 kDa polypeptide, which does not. This triplet of polypeptides, which we refer to as KRP(85/95), binds to purified sea urchin egg tubulin in an AMPPNP-enhanced, ATP-sensitive manner and induces the formation of microtubule bundles. We therefore propose that the triplet corresponds to a novel sea urchin egg kinesin-related protein.

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10

van Berkel, J., M. Steup, W. Völker, H. Robenek, and U. I. Flügge. "Polypeptides of the chloroplast envelope membranes as visualized by immunochemical techniques." Journal of Histochemistry & Cytochemistry 34, no. 5 (May 1986): 577–83. http://dx.doi.org/10.1177/34.5.3517143.

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The polypeptides of relative molecular masses (Mr) 22,000, 29,000, and 36,000 represent three major constituents of the chloroplast envelope of spinach (Spinacia oleracea L.) leaves. The Mr 22,000 polypeptide has been localized in the outer membrane, whereas the two other peptides have been attributed to the inner envelope membrane (Joyard et al., 1983). The Mr 29,000 polypeptide has been identified as the "phosphate translocator" (Flügge and Heldt, 1979). In this investigation, we studied the three envelope polypeptides by means of immunocytochemistry. Using indirect immunofluorescence, all three polypeptides were visualized in cryostat sections of formaldehyde-fixed leaf tissue. They were found in both palisade and spongy parenchyma cells and in guard cells, as indicated by a strong fluorescence in the chloroplast periphery. In contrast, fluorescein isothiocyanate or protein A-gold labeling of isolated fixed chloroplasts resulted only in visualization of the Mr 22,000 polypeptide, a constituent of the outer membrane. We further studied the morphological distribution and frequency of this peptide by electron microscopic evaluation of platinum-carbon replicas after freeze-etching or label-fracture and of ultra-thin sections. By use of these three methods, the polypeptide was found to be randomly distributed in the outer envelope membrane and easily accessible to the immunomarker. Average marker density, as obtained by freeze-etching and label-fracture, was approximately 130 gold particles per square micron.

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Dissertations / Theses on the topic "Polypeptides. Peptides"

1

Meillon, Jean Christophe. "Transport transmembranaire et auto-assemblage impliquant des peptides synthétiques modifiés." Sherbrooke : Université de Sherbrooke, 1998.

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Mehlin, Christopher. "The isolation and characterization of inflammatory polypeptides from Staphylococcus epidermidis /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/9280.

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3

Stark, Margareta. "Isolation and characterization of lipid-associated and neurosecretory polypeptides /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4202-1/.

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4

Zholobko, Oksana. "Functional Colloids from Amphiphilic Polymer Assemblies and Peptides/Polypeptides." Diss., North Dakota State University, 2019. https://hdl.handle.net/10365/29963.

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The use of responsive polymers, where even minor changes in one of the macromolecular characteristics triggered by the external stimuli can cause drastic changes in the material function or performance, is widely studying area of research. Formation of the thermodynamically stable polymer-peptide colloids, such as mixed micellar assemblies or polymer-enzyme conjugates, loading capacity of the colloids, and cargo activity all depend on the macromolecular interactions within the peptide/polypeptide-polymer system. The goal of this work is to investigate interactions between range of new polymers and various cargo molecules and determine whether those interactions affect the physicochemical properties of the resulted colloids. For this purpose, two types of colloid systems were explored: i) peptide-loaded invertible micellar assemblies (IMAs), formed using hydrophobic interactions between amphiphilic invertible polymers (AIP) and peptides (HA, V5, or peptide-based vaccine), and ii) polymeric cellulosomes made from polymer ligand (PL), copolymer of glycidyl methacrylate (GMA) and poly(ethylene glycol) methyl ether methacrylate (PEGMA) and mixture of cellulases, using covalent bonding. The purpose of the research was to evaluate if colloids properties are affected by changes in responsive polymer characteristics as well as if the developed macromolecular structure and composition need further synthetic modification/optimization. AIP-related part of this dissertation is focused on i) understanding of interaction between peptides and AIPs, and formation of mixed micellar assemblies; ii) further behavior of cargo peptide molecules in the micellar interior under the AIP conformational changes, triggered by IMAs localization at polar and nonpolar interface; iii) evaluation of the impact of IMAs on model lipid membrane diffusivity and permeability. Besides, AIP-peptide assemblies were tested in vitro and in vivo in order to evaluate the cargo delivery, antibody response, and immunity protection in vaccinated pigs against Swine influenza viruses (SIV). To explore the feasibility of covalent bonding in formation of responsive polymer-based colloids, enzyme-polymer conjugates (EPCs) were designed and their enzymatic catalytic activity for the biomass hydrolysis was further tested. The effect of conjugation on catalytic activity, conjugation efficiency, glucose inhibition effect, type of substrate, and type of biomass pretreatment were evaluated and compared to free enzymes.
North Dakota. Department of Commerce
National Science Foundation (U.S.)

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5

Cutts, Rosalind Jennifer. "Modelling, NMR and synthesis of food peptides." Thesis, University of Surrey, 1996. http://epubs.surrey.ac.uk/842985/.

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The work in this thesis can be divided into two sections, namely the study of delicious peptide, a food flavour and the antimicrobial peptide lactofenicin B. The main interest in these compounds is in terms of structure and conformation adopted in solution and how this relates to their mode of action. Delicious peptide was studied initially by 1H NMR spectroscopy for evidence of a specific solution structure. Results show that delicious peptide does not adopt a regular conformation in solution. Molecular dynamics simulations of this peptide show the flexibility of the peptide structure in solution. Quenched molecular dynamics simulations were used to search for low energy conformers of the peptide. The results suggest that the flavour of the peptide is produced by interaction of basic and acidic regions in the peptide. The work was extended to examine delicious peptide analogues with similar flavour characteristics. The results obtained suggest that similar interactions of basic and acidic regions occur for these peptides to produce a savoury flavour. The antimicrobial peptide Lactofemcin B was synthesised by Fmoc poly-amide synthesis. Problems with the synthesis occurred due to the protecting groups used for the five arginine residues present in the sequence. Predictive modelling studies on Lactofenicin B peptide, derived from bovine lactofenicin protein suggest that the peptide adopts a region of alpha-helical conformation in solution. The flexibility of the peptide was studied by molecular dynamics in solution and simulations of other environmental conditions were carried out by variation of electrostatic interactions using dielectric constants for membrane, TFE and water environments. The results suggest the beta-helical conformation is most stable in an environment such as trifluoroethanol, the peptide showing more flexibility in aqueous solution. Experimental results for the peptide confirm the flexibility of the peptide in solution. CD results show that lactofenicin B has no specific conformation in solution, although an beta-helical conformation is adopted in trifluoroethanol. The peptide also adopts a beta-sheet conformation in low concentrations of SDS micelle and therefore its conformation is dependant on environmental conditions. NMR studies show that the peptide, although flexible in solution, shows short-range NOE interactions that suggest a local beta-helical conformation may be present. However the overall conformation for the peptide is a flexible one.

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Agut, Willy Lecommandoux Sébastien Taton Daniel. "Conception de nano-objets adaptatifs à base de polypeptides." S. l. : Bordeaux 1, 2008. http://ori-oai.u-bordeaux1.fr/pdf/2008/AGUT_WILLY_2008.pdf.

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7

Fesinmeyer, Robert Matthew. "Chemical shifts define the structure and folding thermodynamics of polypeptides /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/11621.

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8

Lundh, Ann-Christin. "The rational design of catalytically active polypeptides with supersecondary structure." Göteborg : Department of Organic Chemistry, University of Göteborg, 1995. http://catalog.hathitrust.org/api/volumes/oclc/39066015.html.

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9

Charati, Manoj B. "Peptides and polypeptides as scaffolds for optoelectronics and biomaterials applications." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 200 p, 2009. http://proquest.umi.com/pqdweb?did=1891590581&sid=3&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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10

Bergsson, Gudmundur. "Antimicrobial polypeptides and lipids as a part of innate defense mechanism of fish and human fetus /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-546-1/.

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Books on the topic "Polypeptides. Peptides"

1

L, Howell S., and Taylor K. W, eds. The biochemistry of the polypeptide hormones. Chichester: Wiley, 1985.

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2

Gideon, Goldstein, Bach Jean-François, and Wigzell Hans 1938-, eds. Immune regulation by characterized polypeptides: Proceedings of an Ortho-UCLA Symposium held in Steamboat Springs, Colorado, January 25-February 1, 1986. New York: Liss, 1987.

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Innovation and Perspectives in Solid Phase Synthesis (Symposium) (1st 1989 Oxford). Innovation and perspectives in solid phase synthesis: Peptides, polypeptides and oligonucleotides : macro-organic reagents and catalysts : collected papers, first international symposium, August 29- September 2, 1989. Edited by Epton Roger. Birmingham: SPCC(UK), 1990.

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Polypeptide hormone receptors. New York: Dekker, 1985.

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G, Rosselin, ed. International Symposium on Vasoactive Intestinal Peptide Pituitary Adenylate Cyclase Activating Polypeptide & Related Regulatory Peptides: From molecular biology to clinical applications : Euroconference, Strasbourg (Bischenberg), 19-23, September 1993. Singapore: World Scientific, 1994.

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6

Hubert, Vaudry, and Laburthe Marc, eds. VIP, PACAP, and related peptides: From gene to therapy. Boston, Mass: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2006.

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Satkunarajah, Malathy. Studies of the incretins, glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide, and their receptors. Ottawa: National Library of Canada, 1998.

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Mooney, Mark H. Glucagon-like peptide-1 and gastric inhibitory polypeptide: Effects of N-terminal glycation on hormone degradation, insulin secretion and antihyperglycaemic activity. [S.l: The Author], 2000.

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9

Synthetic Polypeptides as Antigens. Elsevier Science & Technology, 1988.

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10

Eysenck. Polypeptide Protein Drugs. Taylor & Francis, 1991.

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Book chapters on the topic "Polypeptides. Peptides"

1

Yasui, Sritana C., and Timothy A. Keiderling. "Vibrational circular dichroism of aromatic polypeptides." In Peptides, 90–92. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_26.

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Fraser, Paul E., and Charles M. Deber. "Modulation of membrane morphology by basic proteins and polypeptides." In Peptides, 60–61. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_15.

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Cole, Alexander M., and Amy Liese Cole. "Dichotomous Roles of Cationic Polypeptides Targeting HIV." In Antimicrobial Peptides, 115–27. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24199-9_8.

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Jung, Günther, Rolf-Peter Hummel, Klaus-Peter Voges, Klaus Albert, and Claudio Toniolo. "13C NMR T1 studies and enantiotopomerisations of 310-helical polypeptides." In Peptides, 37–38. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_7.

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Reynaud, J. A., A. Brack, J. P. Grivet, and Y. Trudelle. "Interaction of phospholipid vesicles with basic amphiphilic polypeptides." In Peptides 1990, 490–92. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_205.

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Ismail, Nurzian, Rickard Hedman, Nina Schiller, Florian Cymer, Ola Nilsson, and Gunnar von Heijne. "Arrest Peptides as Force Sensors to Study Co-translational Membrane Protein Biogenesis." In Regulatory Nascent Polypeptides, 279–90. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_16.

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Chakrabartty, Avijit, Choy L. Hew, Daniel Yang, and Martin Sax. "Action of alanine-rich antifreeze polypeptides: Dipole moment of α-helix for ice recognition." In Peptides, 32–34. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_5.

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Sadat-Aalaee, Dean. "Chemical Synthesis of Peptides and Polypeptides." In Protein-Based Materials, 3–35. Boston, MA: Birkhäuser Boston, 1997. http://dx.doi.org/10.1007/978-1-4612-4094-5_1.

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Hudecz, Ferenc. "Branched polymeric polypeptides with poly[Lys]." In Amino Acids, Peptides and Proteins, 44–90. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788013857-00044.

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Nishino, N., T. Uchida, Y. Ide, and T. Fujimoto. "Catalytic molten globules: Four α-helix bundle polypeptides with catalytic function." In Peptides 1994, 81–82. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_28.

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Conference papers on the topic "Polypeptides. Peptides"

1

Fulcher, C. A., R. A. Houghten, S. de Graaf Mahoney, J. R. Roberts, and T. S. Zimmerman. "SYNTHETIC PEPTIDE PROBES OF FACTOR VIII IMMUNOLOGY AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644768.

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In order to develop specific immunologic reagents for mapping functionally important sites on FVIII, we have prepared rabbit polyclonal antibodies against synthetic peptides of FVIII derived from regions along the entire FVIII amino acid sequence. To date, a total of 70 peptides have been synthesized and characterized by amino acid and HPLC analysis. The peptides were coupled to keyhole limpet hemocyanin with glutaraldehyde as a linkage reagent and used to immunize rabbits. Antisera were tested by ELISA assay on polystyrene microtiter plates coated with either the peptide immunogen, or purified FVIII. The antisera were also tested for their ability to inhibit FVIII clotting activity and to react with separated FVIII polypeptides on immunoblots.Of the 70 peptides, all reacted with the peptide immunogen, 45 reacted with purified FVIII and 33 reacted with FVIII on immunoblots. Because we had obtained evidence that cleavage of the amino terminal region of the 80 kDa polypeptide may play a role in FVIII activation by thrombin, a series of partially overlapping peptides, 15 residues in length, were synthesized in this area. After affinity purifying these antibodies on columns of FVIII immobilized on agarose, adjusting the antibodies to equal antigen binding titers by dot immunoblotting and testing for inhibition of FVIII activity, only one antibody could strongly inhibit FVIII clotting activity. This inhibition could be blocked by the peptide itself at nanomolar concentrations and no significant inhibition could be shown by antibodies to partially overlapping peptides individually, or in combination. These data suggest that a site important to FVIII function can be localized to a 15 amino acid residue region of the 80 kDa polypeptide of FVIII. In addition, a second inhibitoryantibody was identified which was produced against a peptide in the carboxy terminal region of the 54 kDa thrombin fragment of FVIII and this area is currently being studied in a similar manner. In addition, two monoclonal anti-FVIII synthetic peptide antibodies have been produced which react with purified FVIII on immunoblots. One of these antibodies also functions as an immunoadsorbent when linked to agarose and FVII can be purified in this manner, using the synthetic peptide as eluant. It is evident that antibodies to synthetic peptides of FVIII can be useful probes of FVIII structure, function and interactions as well as being of use in FVIII purification.

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2

Pancham, N., M. Dumas, J. Brown, T. C. Michaud, and W. J. Knowles. "SYNTHETIC PEPTIDE ANTIBODIES RECOGNIZE PLASMA AND RECOMBINANT FVIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644027.

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Monoclonal antibodies were raised against synthetic peptides corresponding to the N-termini of the 90kd and 80kd subunits of human FVIII. Preliminary screening was performed directly against the peptides (linked to albumin) coated onto polystyrene wells. IgG was purified by Protein A-Sepharose and affinity purified using the immunogen peptides linked to Sepharose. Immunoreactivity with both plasma and recombinant FVIII was compared by Western blotting, two-site ELISA employing a neutralizing rabbit anti-FVIII IgG as capture antibody, and inhibition in a fluid phase FVIII activity assay. None of the antibodies neutralized clotting or amidolytic activities associated with either FVIII protein. All of the antibodies immunoblotted intacl or thrombin digested FVIII polypeptides according to their anticipated epitope recognition sites; this was useful in determining identity between the two types of FVIII protein. Furthermore, when either FVIII protein was bound to polyclonal IgG coated onto polystyrene microtiter wells, the 80kd antipeptide antibody was capable of detecting both antigens with equal affinity. These results, coupled with results using the 90k antipeptide suggest that epitope accessibility for these antipeptide antibodies is the same for plasma and recombinant FVIII under the conditions tested.

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3

Fay, P. J., S. I. Chavin, and F. J. Walker. "INACTIVATION OF FACTOR VIII BY ACTIVATED PROTEIN C AND PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644770.

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Human factor VIII has been isolated from factor VIII concentrates. The isolated protein is composed of a heavy chain and light chain. The heavy chain was heterogenous with respect to molecular weight ranging from 110-170 kDa. The light chain appeared as a 81/84 kDa dimer, 'when factor VIII was treated with activated protein C in the presence of calcium and phospholipids factor VIII procoagulant activity was rapidly lost. Analysis of the activated protein C catalyzed cleavage products of factor VIII indicated that loss of activity was correlated with cleavage of the heavy chains. The heavy chains appeared to be converted into 93 kDa and 53 kDa peptides. A separate factor VIII preparation has been prepared that contained only a 93 kDa heavy chain as well as the 81/83 kDa light chain. When this preparation was inactivated with activated protein C, a pathway in which the 93 kDa peptide was degraded into a 68 kDa peptide which was subsequently degraded into 48 and 23 kDa polypeptides. This result suggested that the 53 kDa polypeptide was not derived from the 93 kDa domain of the heavy chain, but must have been derived from the variable molecular weight portion of the heavy chain. These results suggest that activated protein C catalyzed a minimum of four cleavages in the heavy chain. Activated protein C did not appear to alter the factor VIII light chain. Protein S has been observed to be a protein cofactor both the anticoagulant and proteolytic action of activated protein C with factor Va. It is thought that protein S forms a lipid bound complex with activated protein C which then can rapidly inactivate factor Va. When factor VIII was inactivated in the presence of both activated protein C and protein S the rate of activity loss was enhanced. The effect of protein S could be observed on the cleavage of the heavy chains and on secondary cleavages of the smaller products including the 93, 68, and 53 kDa polypeptides. In an analogous reaction, the addition of factor Xa has been observed to inhibit the inactivation of factor Va by activated protein C. The addition of factor IX to the factor Vlll-activated protein C reaction mixture resulted in the inhibition of factor VIII inactivation. The effect of factor IX was dose dependent. Finally, as both factor Va and factor VIII have structural similarities and are substrates for activated protein C the possibility that they might compete as substrates was tested. Factor VIII was observed to compete with factor Va for activated protein C. The concentration dependence of factor VIII inhibition of factor Va inactivation suggested that factor VIII and factor Va were equivalent substrates for activated protein C.

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4

Pancham, N., M. Dumas, M. S. Madant, P. C. Esmon, and V. Voehrinqer. "RECOMBINANT AND PLASMA FVIII SHARE EPITOPES RECOGNIZED BY A PANEL OF MONOCLONAL AND POLYCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644028.

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A panel of neutralizing and nonneutralizing monoclonal and polyclonal antibodies raised against human plasma FVIII and human recombinant FVIII was employed in Western blotting, activity inhibition and two-site ELISA studies to investigate structural similarities between recombinant FVIII (r-FVIII) and plasma FVIII (p-FVIII). The monoclonal antibodies were obtained either commercially or produced in-house and react with either the 90kd, 80kd or B-region polypeptides. Some antibodies were raised to FVIII synthetic peptides. Rabbit polyclonal antibodies were obtained from either r-FVIII or p-FVIII immunizations. Recombinant FVIII and p-FVIII were compared either as intact molecules or following thrombin digestion by immunoblots after SDS gradient PAGE. Combinations of antibodies were used in two-site ELISA. Activity inhibition was evaluated by one-stage clotting or in FXa generation assays. Recombinant FVIII and p-FVIII responded similarly to these antibodies in all of the immunotechniques used. Collectively, these results indicate that using this approach r-FVIII and p-FVIII display similar structural and functional characteristics.

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5

Rosselin, Gabriel. "Vasoactive Intestinal Peptide Pituitary Adenylate Cyclase Activating Polypeptide and Related Regulatory Peptides." In International Symposium on Vasoactive Intestinal Peptide Pituitary Adenylate Cyclase Activating Polypeptide and Related Regulatory Peptides. WORLD SCIENTIFIC, 1994. http://dx.doi.org/10.1142/9789814534222.

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6

Flegel, Martin. "Polypeptide laboratories – Development and production of peptides as drugs." In VIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199903001.

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7

Sancova, Katerina, Lucie Bednarova, Romana Sulakova, Sergej Karel, Barbora Brtkova, Martin Flegel, and Vladimr Velebn. "Modulation of the properties of elastin-like polypeptides by structure variations." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.188.

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8

Hudecz, Ferenc. "Immunorecognition of epitope peptides modified by flanking or conjugation to branched polypeptide carrier." In VIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2001. http://dx.doi.org/10.1135/css200104007.

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9

Brennan, S. O., P. M. George, R. W. Carrel, and R. Jordan. "THE PHYSIOLOGICAL ANTITHROMBIN (BETA) VARIANT WITH INCREASED HEPARIN AFFINITY LACKS CARBOHYDRATE AT ASN 135." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643680.

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Some 10% of the antithrombin fromnormal human plasma can be isolated onthe basis of its higher affinity forheparin Sepharose. Not only does this ATIII beta have a higher heparinaffinity, but it is also less negatively charged and has a lower molecular weight than normal AT-III alpha.Neuraminidase and Endo F treatment suggest the loss of a single carbohydrate sidechain from beta AT-III (Peterson and Blackburn. J Biol Chem 1985,260, 610)Antithrombin has a single polypeptide chain with biantennary carbohydrate attachment sites at asparagines 96, 135, 155 and 172. The 25 kDA CNBr fragment of AT-III alpha (residues 104-251) runs at 22.5kDa in the case of AT-III beta yet they have the same N and C-terminal sequence. Tryptic peptide maps of theseCNBr fragments showed that a single neutral (glyco) peptide, Lys-Ala-Asn⋆-Lys was missing from AT-III beta and replaced by twobasic peptides, Lys, Ala, Asn, Lys and Ala, Asn, Lys; indicating the absence of an oligosaccharide sidechainon asparagine 135. This was confirmed by chromatography of tryptic peptides on Con A-Sepharose followed by mapping of the bound and unbound fractions. There were two new unbound peptides (Lys, Ala, Asn, Lys and Ala, Asn, Lys) in AT-III beta. The corresponding peptide Lys-Ala-Asn⋆-Lys was the only peptide missing from the bound glycopeptide fraction.The absence of carbohydrate at Asn 135 explains the increased heparinaffinity of beta AT-III as on the molecular model this oligosaccharide forms a negative and bulky shell on the perimeter of the positive bindingsite centred on Arg 47.Whether the loss of the sidechain is due to circulatory removal is not known but a recent variant identification confirmsthat it may alternatively be due to failure of attachment at the time ofsynthesis. Potentially the loss or modification of oligosaccharide 135 provides another level of control of coagulation by altering the avidity of AT-III for thrombin when heparin activation is suboptimal.

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Sonzini, Silvia, Frank Biedermann, and Oren A. Scherman. "Synthesis of Photoswitchable Homodimeric Polypeptides: Towards Biological Applications." In The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.244.

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Reports on the topic "Polypeptides. Peptides"

1

Garrison, W. M. Reaction mechanisms in the radiolysis of peptides, polypeptides and proteins. Office of Scientific and Technical Information (OSTI), January 1985. http://dx.doi.org/10.2172/5415209.

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2

Storrs, R. W. Structural studies of polypeptides: Mechanism of immunoglobin catalysis and helix propagation in hybrid sequence, disulfide containing peptides. Office of Scientific and Technical Information (OSTI), August 1992. http://dx.doi.org/10.2172/6707762.

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3

Storrs, Richard Wood. Structural studies of polypeptides: Mechanism of immunoglobin catalysis and helix propagation in hybrid sequence, disulfide containing peptides. Office of Scientific and Technical Information (OSTI), August 1992. http://dx.doi.org/10.2172/10131755.

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4

Bidwell, III, and Gene L. Thermally Targeted Delivery of a c-Myc Inhibitory Peptide In Vivo Using Elastin-like Polypeptide. Fort Belvoir, VA: Defense Technical Information Center, October 2009. http://dx.doi.org/10.21236/ada525489.

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5

Arnett, Clint, Justin Lange, Ashley Boyd, Martin Page, and Donald Cropek. Expression and secretion of active Moringa oleifera coagulant protein in Bacillus subtilis. Engineer Research and Development Center (U.S.), August 2021. http://dx.doi.org/10.21079/11681/41546.

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Cationic polypeptide proteins found in the seeds of the tropical plant Moringa oleifera have coagulation efficiencies similar to aluminum and ferric sulfates without their recalcitrant nature. Although these proteins possess great potential to augment or replace traditional coagulants in water treatment, harvesting active protein from seeds is laborious and not cost-effective. Here, we describe an alternative method to express and secrete active M. oleifera coagulant protein (MO) in Bacillus subtilis. A plasmid library containing the MO gene and 173 different types of secretory signal peptides was created and cloned into B. subtilis strain RIK1285. Fourteen of 440 clones screened were capable of secreting MO with yields ranging from 55 to 122 mg/L of growth medium. The coagulant activity of the highest MO secreting clone was evaluated when grown on Luria broth, and cell-free medium from the culture was shown to reduce turbidity in a buffered kaolin suspension by approximately 90% compared with controls without the MO gene. The clone was also capable of secreting active MO when grown on a defined synthetic wastewater supplemented with 0.5% tryptone. Cell-free medium from the strain harboring the MO gene demonstrated more than a 2-fold reduction in turbidity compared with controls. Additionally, no significant amount of MO was observed without the addition of the synthetic wastewater, suggesting that it served as a source of nutrients for the effective expression and translocation of MO into the medium.

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