5H1I
NMR structure of TIBA, a chimera of SFTI
Summary for 5H1I
| Entry DOI | 10.2210/pdb5h1i/pdb |
| Related | 5H1H |
| NMR Information | BMRB: 36024 |
| Descriptor | Bradykinin-trypsin inhibitor secondary loop chimera (1 entity in total) |
| Functional Keywords | tiba, chimera, sunflower trypsin inhibitor, cyclic peptide, de novo protein |
| Biological source | Helianthus annuus |
| Total number of polymer chains | 1 |
| Total formula weight | 1944.39 |
| Authors | |
| 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 Cited by 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: 27977181DOI: 10.1021/acs.jmedchem.6b01011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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