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Conformational study of a somatostatin analogue in DMSO/water by 2D NMR by Patricia Verheyden; Wim Francq; Henri Pepermans; Georges Van Binst is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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NMH studies of numerous somatostatin analogues have shown that all those showing biological activity adopt a o,, I turn-6 sheet conformation in dimethylsulfoxide (DMSO ) solution, but that this is not a sufficient condition for biological In this communication, we demonstrate that this backbone conformation is conserved in different solvents, and, consequently, we postulate that this conformation might be adopted at the receptor also. We performed this study on the analogue DC13-116 ( ~~Nal~-Cys~-Tyr~-DTrp~-Lys~-Val'~-Cys "-Thr "-NHz, numbering as in native somatostatin), a highly active somatostat in analogue in the GH release inhibitory This analogue is expected t o have a constrained conformation due to its reduced sizeg ( 8 amino acids out of 14 in native somatostatin), the cyclization between the two cysteins,"' and the replacement of LTrp in position 8 by 1)Trp." Measurements done previously by our group on DC13-11 6 in water solution' indicated a different conformation. This conformation proposal was based mainly on measurements of the temperature dependence of the chemical shifts of the amide protons ( A 6 N H / A T measurements), which contained a systematic error, due to

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Author

Patricia Verheyden; Wim Francq; Henri Pepermans; Georges Van Binst

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1990

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)