Issue 4, 2007

Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and l-Ala as building blocks

Abstract

Residue based control of specific helical folding is explored in hybrid peptide oligomers consisting of alternating L-Ala and cis-β-furanoid sugar amino acid (FSAA) residues as building blocks; two series of these hybrid oligomers are designed, synthesized and extensively characterized by using NMR, CD, FT-IR and MD simulation studies; results show the co-existence of left-handed 11- and 14/15-helical conformations in these short oligomers of Boc-(α/β) and Boc-(β/α) series.

Graphical abstract: Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and l-Ala as building blocks

Supplementary files

Article information

Article type
Communication
Submitted
22 Aug 2006
Accepted
10 Nov 2006
First published
07 Dec 2006

Chem. Commun., 2007, 371-373

Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and L-Ala as building blocks

B. Jagadeesh, A. Prabhakar, G. D. Sarma, S. Chandrasekhar, G. Chandrashekar, M. S. Reddy and B. Jagannadh, Chem. Commun., 2007, 371 DOI: 10.1039/B612058J

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