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Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membraneA 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.
Document ID
20050000485
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Zhang, S.
(Massachusetts Institute of Technology Cambridge 02139)
Holmes, T.
Lockshin, C.
Rich, A.
Date Acquired
August 22, 2013
Publication Date
April 15, 1993
Publication Information
Publication: Proceedings of the National Academy of Sciences of the United States of America
Volume: 90
Issue: 8
ISSN: 0027-8424
Subject Category
Exobiology
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Program Exobiology
NASA Discipline Number 52-20
NASA Discipline Exobiology

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