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A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight

By S. Guha, M.G.B. Drew and A. Banerjee

Abstract

A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located beta-alanine residue, beta-alanyl-L-valine (1), beta-alanyl-L-isoleucine (2), and beta-alanyl-L-phenylalanine (3, form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned beta-alanine containing dipeptide (4), L-phenylalanyl-beta-alanine, does not form a supramolecular double helical structure. beta-Ala-Xaa (Xaa = Val/Ile/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state

Year: 2007
DOI identifier: 10.1021/ol0701870
OAI identifier: oai:centaur.reading.ac.uk:11292
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