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- W2144610999 abstract "BQ123 is a cyclic pentapeptide and a potent endothelin-1 inhibitor. The crystal structure of the BQ123 sodium salt was determined as the first example of an endothelin inhibitor. Four independent molecules and many solvent molecules were found in the asymmetric unit; the total weight was about 3000 Da. The precise structure including the solvent molecules was determined using high-resolution data collected on a synchrotron source. Sodium ions formed unique structures with five and six coordination bonds and their forms were distinguished into three classes. An ion was sandwiched by two BQ123 molecules. This peptide-sodium (2:1) complex showed a cage-like structure and octahedral coordination was observed. Sodium ions also formed a cluster composed of hydrated water molecules and peptides. Two sodium ions were contained in this cluster, making five coordination bonds. Despite having the same coordination numbers, these ions were distinguishable by differences in the polyhedra. One was trigonal bipyramidal (having six planes) and the other was square pyramidal (having five planes). Both shapes were very similar to each other, although the synchrotron data clearly revealed slight geometrical differences." @default.
- W2144610999 created "2016-06-24" @default.
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- W2144610999 date "2001-04-24" @default.
- W2144610999 modified "2023-10-18" @default.
- W2144610999 title "Caged and clustered structures of endothelin inhibitor BQ123, cyclo(-<scp>D</scp>-Trp-<scp>D</scp>-Asp<sup>−</sup>-Pro-<scp>D</scp>-Val-Leu-)cdotNa<sup>+</sup>, forming five and six coordination bonds between sodium ions and peptides" @default.
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- W2144610999 doi "https://doi.org/10.1107/s0907444901002797" @default.
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