Structural highlights
Publication Abstract from PubMed
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-NH2 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, Zn(2+) and Cd(2+), 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.
A previously undescribed hexapeptide His-Arg-Phe-Leu-Arg-His-NH2 from amphibian skin secretion shows CO2 and metal biding affinities.,Pires DAT, Arake LMR, Silva LP, Lopez-Castillo A, Prates MV, Nascimento CJ, Bloch C Jr Peptides. 2018 Jun 19;106:37-44. doi: 10.1016/j.peptides.2018.06.003. PMID:29933027[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pires DAT, Arake LMR, Silva LP, Lopez-Castillo A, Prates MV, Nascimento CJ, Bloch C Jr. A previously undescribed hexapeptide His-Arg-Phe-Leu-Arg-His-NH2 from amphibian skin secretion shows CO2 and metal biding affinities. Peptides. 2018 Jun 19;106:37-44. doi: 10.1016/j.peptides.2018.06.003. PMID:29933027 doi:http://dx.doi.org/10.1016/j.peptides.2018.06.003
