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

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Issued Date

2015

Resource Type

Article

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application/pdf

ISSN

13877003

DOI

10.1016/j.inoche.2015.03.037

Other identifier(s)

2-s2.0-84925302505

Rights Holder(s)

Scopus

Bibliographic Citation

Inorganic Chemistry Communications. Vol 55, (2015), p.129-131

Suggested Citation

Jityuti B., Buranaprapuk A., Liwporncharoenvong T. Artificial metallopeptidases: Protein cleavage by molybdenum(VI) peroxo α-amino acid complexes. Inorganic Chemistry Communications. Vol 55, (2015), p.129-131. doi:10.1016/j.inoche.2015.03.037 Retrieved from: https://hdl.handle.net/20.500.14740/6241

Title

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

Author(s)

Jityuti B.
 Buranaprapuk A.
 Liwporncharoenvong T.

Abstract

Three molybdenum(VI) peroxo α-amino acid complexes, MoO(O2)2(α-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(O2)2(α-aa) (H2O)-protein mixture at 37°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. © 2015 Elsevier B.V. All rights reserved.

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URI

https://hdl.handle.net/20.500.14740/6241

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Scopus: Year 1983-2021

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