Structural highlights
Publication Abstract from PubMed
An orally active and metabolically stable peptide TIBA was successfully engineered as a chimera by fusing an analgesic bradykinin receptor antagonist peptide and the trypsin inhibitory loop of sunflower trypsin inhibitor-1. As a fusion cyclic peptide, the metabolically labile analgesic peptide is protected from degradation by exopeptidases as well as the endopeptidases, and its serum half-life extended from <5 min to >6 h as a chimera. Moreover, the chimera TIBA was also found to be orally active in an animal pain model using a hot plate assay.
An Orally Active Bradykinin B1 Receptor Antagonist Engineered as a Bifunctional Chimera of Sunflower Trypsin Inhibitor.,Qiu Y, Taichi M, Wei N, Yang H, Luo KQ, Tam JP J Med Chem. 2017 Jan 12;60(1):504-510. doi: 10.1021/acs.jmedchem.6b01011. Epub, 2016 Dec 15. PMID:27977181[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qiu Y, Taichi M, Wei N, Yang H, Luo KQ, Tam JP. An Orally Active Bradykinin B1 Receptor Antagonist Engineered as a Bifunctional Chimera of Sunflower Trypsin Inhibitor. J Med Chem. 2017 Jan 12;60(1):504-510. doi: 10.1021/acs.jmedchem.6b01011. Epub, 2016 Dec 15. PMID:27977181 doi:http://dx.doi.org/10.1021/acs.jmedchem.6b01011
