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

Guha, S., Drew, M.G.B. and Banerjee, A. (2007) A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight. Organic Letters, 9 (7). pp. 1347-1350. ISSN 1523-7060

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To link to this item DOI: 10.1021/ol0701870

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11292
Uncontrolled Keywords:HYDROPHOBIC DIPEPTIDES, DIMERIZATION, STRANDS, CHAINS, WATER

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