1. A previously undescribed hexapeptide His-Arg-Phe-Leu-Arg-His-NH 2 from amphibian skin secretion shows CO 2 and metal biding affinities.
- Author
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Pires DAT, Arake LMR, Silva LP, Lopez-Castillo A, Prates MV, Nascimento CJ, and Bloch C Jr
- Subjects
- Amphibian Proteins isolation & purification, Animals, Binding Sites, Cadmium chemistry, Ligands, Oligopeptides isolation & purification, Protein Conformation, Zinc chemistry, Amphibian Proteins chemistry, Anura physiology, Carbon Dioxide chemistry, Cations, Divalent chemistry, Oligopeptides chemistry, Skin metabolism
- Abstract
A previously undescribed six residues long peptide His-Arg-Phe-Leu-Arg-His was identified and purified from the skin secretion of the amphibian Phyllomedusa centralis. A synthetic analogue carboxyamidated HRFLRH-NH
2 showed structural changes induced by CO2 and metal ions in aqueous solution when analyzed by NMR. The present work reports NMR structures for the carboxyamidated hexapeptide in the presence CO2 , Zn2+ and Cd2+ , suggesting possible affinity regions on the polypeptide chain for each ligand. The NMR structures were optimized by DFT to identify probable biding sites of these species in the polypeptide structure. To our best knowledge, this is the first time that a putative CO2 binding site is described on a peptide structure obtained in aqueous conditions, at room temperature., (Copyright © 2018 Elsevier Inc. All rights reserved.)- Published
- 2018
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