5H1H

NMR structure of SLBA, a chimera of SFTI

Summary for 5H1H

• Entry DOI: 10.2210/pdb5h1h/pdb
• Related: 5H1I
• NMR Information: BMRB: 36023
• Descriptor: Bradykinin-trypsin inhibitor secondary loop chimera (1 entity in total)
• Functional Keywords: slba, sunflower trypsin inhibitor, cyclic peptide, disulphide bond, de novo protein
• Biological source: Helianthus annuus
• Total number of polymer chains: 1
• Total formula weight: 1780.10

Authors

Xiao, T.,Tam, J.P. (deposition date: 2016-10-10, release date: 2017-04-19, Last modification date: 2024-11-20)

Primary citation

Qiu, Y.,Taichi, M.,Wei, N.,Yang, H.,Luo, K.Q.,Tam, J.P.
An Orally Active Bradykinin B1 Receptor Antagonist Engineered as a Bifunctional Chimera of Sunflower Trypsin Inhibitor.
J. Med. Chem., 60:504-510, 2017

PubMed Abstract: 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.

PubMed: 27977181
DOI: 10.1021/acs.jmedchem.6b01011

Experimental method

SOLUTION NMR