Artificial metallopeptidases: Protein cleavage by molybdenum(VI) peroxo alpha-amino acid complexes

作者：Jityuti Benchawan; Buranaprapuk Apinya; Liw****charoenvong Teerayuth^*

来源：Inorganic Chemistry Communications, 2015, 55: 129-131.

DOI：10.1016/j.inoche.2015.03.037

• Cleavage reactions
• Pepsin
• Molybdenum complexes
• Protein-metal interactions

Three molybdenum(VI) peroxo alpha-amino acid complexes, MoO(O-2)(2)(alpha-aa) (H2O) (aa = leucine, glutamine and glycine), were prepared and used as artificial proteases for site-specific cleavage of porcine pepsin. The reaction was activated by incubation of the MoO(O-2)(2)(alpha-aa) (H2O)-protein mixture at 37 degrees C (2-24 h). All three molybdenum complexes resulted in different cleavage sites, indicating different binding sites on the protein. Charges and the lengths of the amino acid side chains may distribute in the variation of the probe binding sites. The study can provide a new approach for the footprinting of metal binding sites on proteins in the future.

• 出版日期2015-5