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

Guha, Samit ; Drew, Michael G. B. ; Banerjee, Arindam (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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Official URL: http://pubs.acs.org/doi/abs/10.1021/ol0701870

Related URL: http://dx.doi.org/10.1021/ol0701870

Abstract

A series of water-soluble synthetic dipeptides (1−3) with an N-terminally located β-alanine residue, β-alanyl-l-valine (1), β-alanyl-l-isoleucine (2), and β-alanyl-l-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned β-alanine containing dipeptide (4), l-phenylalanyl-β-alanine, does not form a supramolecular double helical structure. β-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.

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ID Code:99584
Deposited On:07 Nov 2016 11:27
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