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Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
Open accessAbstract
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.
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Metadata
- Authors
- Zhang, S., Holmes, T., Lockshin, C., & Rich, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-04-15
- Volume
- 90
- Issue
- 8
- Pages
- 3334-3338
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2001599007
- Cited by
- 1,304
- References
- 0
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- green
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