期刊
BIOPOLYMERS
卷 98, 期 3, 页码 169-184出版社
WILEY
DOI: 10.1002/bip.22058
关键词
peptide self-assembly; amphipathic peptide; fibril; hydrogel; peptide biomaterials
资金
- Alzheimer's Association [NIRG-08-90797]
- American Chemical Society, Petroleum Research Fund [48922-DNI1]
- DuPont (DuPont Young Professor Award)
- Creative and Novel Ideas in HIV Research Program (CNIHR)
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0840410] Funding Source: National Science Foundation
Amphipathic peptides composed of alternating polar and nonpolar residues have a strong tendency to self-assemble into one-dimensional, amyloid-like fibril structures. Fibrils derived from peptides of general (XZXZ)n sequence in which X is hydrophobic and Z is hydrophilic adopt a putative beta-sheet bilayer. The bilayer configuration allows burial of the hydrophobic X side chain groups in the core of the fibril and leaves the polar Z side chains exposed to solvent. This architectural arrangement provides fibrils that maintain high solubility in water and has facilitated the recent exploitation of self-assembled amphipathic peptide fibrils as functional biomaterials. This article is a critical review of the development and application of self-assembling amphipathic peptides with a focus on the fundamental insight these types of peptides provide into peptide self-assembly phenomena. (c) 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 169184, 2012.
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