Gelation Behavior of β-Sheet Peptide RADA16 Coexisting with Synthetic Polymers
نویسندگان
چکیده
منابع مشابه
Well-defined synthetic polymers with a protein-like gelation behavior in water.
Homopolymers of N-acryloyl glycinamide were prepared by reversible addition-fragmentation chain transfer polymerization in water. The formed macromolecules exhibit strong polymer-polymer interactions in aqueous milieu and therefore form thermoreversible physical hydrogels in pure water, physiological buffer or cell medium.
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β-Sheet forming peptides have attracted significant interest for the design of hydrogels for biomedical applications. One of the main challenges is the control and understanding of the correlations between peptide molecular structure, the morphology, and topology of the fiber and network formed as well as the macroscopic properties of the hydrogel obtained. In this work, we have investigated th...
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Nanofiber structures of some peptides and proteins as biological materials have been studied extensively, but their molecular mechanism of self-assembly and reassembly still remains unclear. We report here the reassembly of an ionic self-complementary peptide RADARADARADARADA (RADA16-I) that forms a well defined nanofiber scaffold. The 16-residue peptide forms stable beta-sheet structure and un...
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Objective(s):Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western ...
متن کاملProteolytic stability of amphipathic peptide hydrogels composed of self-assembled pleated β-sheet or coassembled rippled β-sheet fibrils.
Hydrogel networks composed of rippled β-sheet fibrils of coassembled D- and L-Ac-(FKFE)2-NH2 amphipathic peptides exhibit proteolytic stability and increased rheological strength compared to networks of self-assembled L-Ac-(FKFE)2-NH2 pleated β-sheet fibrils. Modifying the ratios of l and d peptides in the coassembled rippled β-sheet fibrils alters the degradation profiles of these hydrogel net...
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ژورنال
عنوان ژورنال: Transactions of the Materials Research Society of Japan
سال: 2010
ISSN: 1382-3469,2188-1650
DOI: 10.14723/tmrsj.35.543