O. Cusinato et al., THE MOLECULAR-CONFORMATIONS OF REPRESENTATIVE ARTHROPOD ADIPOKINETIC PEPTIDES DETERMINED BY CIRCULAR-DICHROISM SPECTROSCOPY, Insect biochemistry and molecular biology, 28(1), 1998, pp. 43-50
The secondary structure of six members of the AKH/RPCH family of arthr
opod neuropeptides has been studied by circular dichroism spectroscopy
, None of the peptides examined shows a clear ordered conformation in
aqueous solution, pH 7.5 at room temperature. At low temperatures in e
thanediol/aqueous buffer (2:1, pH 7.5), however, a P-II extended confo
rmation becomes apparent in all of the peptides tested. For the peptid
es that are most active in the lipid mobilization assay, interaction w
ith SDS micelles induces the formation of a beta-structure. (C) 1998 E
lsevier Science Ltd. All rights reserved.