Conclusions
Fully and partially DPIV-resistant analogs of GIP1–30 could be synthesized. The introduction of D-amino acids in P1- and P1’-position resulted in a slight reduction in binding and bioactivity. The examined C-terminal truncated fragments (with exception of the GIP1–30 fragment) showed no binding affinity, whereas the antagonistic N-terminal truncated fragments were able to bind to transfected rat GIP receptor. These results emphasize the hypothesis of an existing one-receptor-two-interaction-sites-model which was shown for peptides of the GRF-family.
Concerning the potential use of GIP analogs in the treatment of type II diabetes mellitus, these results offer the possibility to synthesize analogs with reasonable half-life times and physiologically relevant binding affinities and bioactivity.
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Kühn-Wache, K. et al. (2002). Analogs of Glucose-Dependent Insulinotropic Polypeptide With Increased Dipeptidyl Peptidase IV Resistance. In: Langner, J., Ansorge, S. (eds) Cellular Peptidases in Immune Functions and Diseases 2. Advances in Experimental Medicine and Biology, vol 477. Springer, Boston, MA. https://doi.org/10.1007/0-306-46826-3_21
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DOI: https://doi.org/10.1007/0-306-46826-3_21
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