In this study, three synthetic zinc-chelating peptides (ZCPs) derived from sea cucumber hydrolysates with limited or none of the common metal-chelating amino-acid residues were analyzed by flame atomic absorption spectroscopy, circular dichroism spectroscopy, size exclusion chromatography, zeta-potential, Fourier transform infrared spectroscopy, Raman spectroscopy and nuclear magnetic resonance spectroscopy. The amount of zinc bound to the ZCPs reached maximum values with ZCP:zinc at 1:1, and it was not further increased by additional zinc presence. The secondary structures of ZCPs were slightly altered, whereas no formation of multimers was observed. Furthermore, zinc increased the zeta-potential value by neutralizing the negatively charged residues. Only free carboxyl in C-terminus of ZCPs was identified as the primary binding site of zinc. These results provide the theoretical foundation to understand the mechanism of zinc chelation by peptides.
Available at: http://works.bepress.com/chenxu_yu/32/
This article is published as Liu, Xiaoyang, Zixu Wang, Fawen Yin, Yuxin Liu, Ningbo Qin, Yoshimasa Nakamura, Fereidoon Shahidi, Chenxu Yu, Dayong Zhou, and Beiwei Zhu. "Zinc-Chelating Mechanism of Sea Cucumber (Stichopus japonicus)-Derived Synthetic Peptides." Marine Drugs 17, no. 8 (2019): 438. DOI: 10.3390/md17080438. Posted with permission.