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Conformation of human little gastrin and minigastrin analogs in surfactant solution
Author(s) -
Mammi S.,
Mammi N. J.,
Foffani M. T.,
Peggion E.,
Moroder L.,
Wünsch E.
Publication year - 1987
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/bip.360260005
Subject(s) - chemistry , gastrin , micelle , aqueous solution , pulmonary surfactant , solubilization , fluorescence , biophysics , stereochemistry , biochemistry , organic chemistry , secretion , physics , quantum mechanics , biology
The conformational properties of the two gastrin analogs, Nle 15 ‐human little gastrin and des‐Trp 1 , Nle 12 ‐human minigastrin, have been investigated in aqueous solution in the presence of increasing amounts of sodium dodecylsulfate (SDS). Both analogs at acidic pH form a β‐structure when the detergent concentration is below the CMC. Above the CMC the hormones assume an ordered conformation characterized by a far‐uv CD pattern with the same shape of that previously observed in trifluoroethanol. Thus, both media support the same structure. CD and fluorescence data suggest that the little gastrin analog is completely solubilized in the interior of the micelles, while the minigastrin analog is only partially solubilized because of the presence of a positive charge at the N‐terminus.