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. 1993 Apr 15;90(8):3334–3338. doi: 10.1073/pnas.90.8.3334

Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.

S Zhang 1, T Holmes 1, C Lockshin 1, A Rich 1
PMCID: PMC46294  PMID: 7682699

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.

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Selected References

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