Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1383713 | Bioorganic & Medicinal Chemistry Letters | 2016 | 6 Pages |
Abstract
Conformational analysis of the CCK-B receptor selective peptide Gly-Trp-N-(Me)Nle-Aps-PheNH2 suggests the possibility of cis-trans isomerization about the Trp-N-(Me)Nle peptide bond. We have described the synthesis of the tryptophan-norleucine containing tetrazole dipeptide TrpΨ[CN4]Nle as a cis amide bond surrogate. The peptide Gly-TrpΨ[CN4]Nle-Asp-PheNH2 had low affinity to the CCK-B receptor. However, the intermediate Boc-TrpΨ[CN4]Nle-Asp-PheNH2 had considerable affinity to the CCK-A receptor.
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Lakmal W. Boteju, Teresa Zalewska, Henry I. Yamamura, Victor J. Hruby,