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Solution structure of dehydropeptides: A CD investigation
Author(s) -
Pieroni O.,
Fissi A.,
Jain R. M.,
Chauhan V. S.
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199601)38:1<97::aid-bip8>3.0.co;2-r
Subject(s) - chemistry
A CD investigation of eleven dehydropeptides is reported. The compounds investigated include tri‐, tetra‐, hexa‐, hepta‐, and octapeptides and contain one, two, or three dehydro‐phenylalanine (ΔPhe) residues. The peptides showed different CD profiles depending on chain length, position, and number of dehydro residues. The CD data very much complemented that provided by nmr studies, confirming the conformational preference for β‐bend structures in small peptides (tripeptides), and 3 10 ‐helical or α‐helical structures in longer peptides. The secondary structures were stable in chloroform solution and were denaturated by addition of trifluoroacetic acid. Solvent titration experiments performed by measuring CD as a function of solvent composition provided evidence that the order →←2 disorder conformational changes occurred as cooperative transitions. © 1996 John Wiley & Sons, Inc.