A preferred conformation in the vasoactive intestinal peptide (VIP). Molecular architecture of gastrointestinal hormones |
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| Authors: | Miklos Bodanszky Agnes Bodanszky Yakir S. Klausner Sami I. Said |
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| Affiliation: | 1. Department of Chemistry, Case Western Reserve University, Cleveland, Ohio 44106 USA;2. Department of Internal Medicine, The University of Texas Southwestern Medical School, Dallas, Texas 75216 USA;3. V.A. Hospital, Dallas, Texas 75216 USA |
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| Abstract: | The ORD spectrum of the vasoactive intestinal peptide (VIP) in water indicates a preferred conformation with low helix content. Addition of organic solvents, especially of trifluoroethanol, results, even at low solvent concentration, in spectra with pronounced helical character. The readiness of shorter chains, with C-terminal sequences of VIP, to take up helical conformation under the effect of organic solvents parallels their biological activity. This suggests that an “active architecture” may be required for the interaction between hormone and receptor. |
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| Keywords: | To whom correspondence should be addressed (CWRU). |
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