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Review self‐assembly of amphipathic β‐sheet peptides: Insights and applications
Author(s) -
Bowerman Charles J.,
Nilsson Bradley L.
Publication year - 2012
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22058
Subject(s) - amphiphile , chemistry , fibril , self assembly , bilayer , peptide , amyloid fibril , side chain , sequence (biology) , biophysics , lipid bilayer , polar , nanotechnology , crystallography , membrane , biochemistry , polymer , organic chemistry , copolymer , amyloid β , materials science , medicine , physics , disease , pathology , astronomy , biology
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 β‐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. © 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 169–184, 2012.