AI Article Synopsis
- The cyclic octapeptide cyclo (Ala-Leu-Pro-Gly)2 exhibits unique conformation and ion-binding properties when studied in acetonitrile using CD and NMR spectroscopy.
- It shows a strong preference for binding to divalent cations like calcium, magnesium, and barium.
- The free peptide and its calcium complex have similar structures, characterized by defined beta- and gamma-turns, and the peptide forms stable complexes in a 1:1 or possibly 2:1 ratio with these cations.
Article Abstract
The conformation and ion-binding characteristics of a cyclic octapeptide, cyclo (Ala-Leu-Pro-Gly)2, in a liphophilic solvent, acetonitrile, have been studied using CD and nmr spectroscopy. The peptide binds preferentially to divalent cations such as calcium, magnesium, and barium. The conformations of the free cyclic peptide and its calcium complex are very similar with well-defined beta- and gamma-turns. The cyclic peptide readily forms equimolar and possibly 2:1 (peptide:cation) complexes with divalent cations.
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| http://dx.doi.org/10.1002/bip.360320810 | DOI Listing |
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