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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 384, Issue 3


Structure-Activity Relationships of Glucose-Dependent Insulinotropic Polypeptide (GIP)

S.A. Hinke / R. Gelling / S. Manhart / F. Lynn / R.A. Pederson / K. Kühn-Wache / F. Rosche / H.-U. Demuth / D. Coy / C.H.S. McIntosh
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.046


Six GIP1-30NH2 analogs were synthesized with modifications (de-protonation, N-methylation, reversed chirality, and substitution) at positions 1, 3, and 4 of the N-terminus, and additionally, a cyclized GIP derivative was synthesized. The relationship between altered structure to biological activity was assessed by measuring receptor binding affinity and ability to stimulate adenylyl cyclase in CHO-K1 cells transfected with the wild-type GIP receptor (wtGIPR). These structureactivity relationship studies demonstrate the importance of the GIP N-terminus and highlight structural constraints that can be introduced in GIP analogs. These analogs may be useful starting points for design of peptides with enhanced in vivo bioactivity.

About the article

Published Online: 2005-06-01

Published in Print: 2003-03-14

Citation Information: Biological Chemistry, Volume 384, Issue 3, Pages 403–407, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.046.

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