| Literature DB >> 7682699 |
S Zhang1, T Holmes, C Lockshin, A Rich.
Abstract
A 16-residue peptide [(Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)2] has a characteristic beta-sheet circular dichroism spectrum in water. Upon the addition of salt, the peptide spontaneously assembles to form a macroscopic membrane. The membrane does not dissolve in heat or in acidic or alkaline solutions, nor does it dissolve upon addition of guanidine hydrochloride, SDS/urea, or a variety of proteolytic enzymes. Scanning EM reveals a network of interwoven filaments approximately 10-20 nm in diameter. An important component of the stability is probably due to formation of complementary ionic bonds between glutamic and lysine side chains. This phenomenon may be a model for studying the insoluble peptides found in certain neurological disorders. It may also have implications for biomaterials and origin-of-life research.Entities:
Keywords: NASA Discipline Exobiology; NASA Discipline Number 52-20; NASA Program Exobiology; Non-NASA Center
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Year: 1993 PMID： 7682699 PMCID： PMC46294 DOI： 10.1073/pnas.90.8.3334
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205