Picture of a black hole

Strathclyde Open Access research that creates ripples...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of research papers by University of Strathclyde researchers, including by Strathclyde physicists involved in observing gravitational waves and black hole mergers as part of the Laser Interferometer Gravitational-Wave Observatory (LIGO) - but also other internationally significant research from the Department of Physics. Discover why Strathclyde's physics research is making ripples...

Strathprints also exposes world leading research from the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

The role of conserved residues of chagasin in the inhibition of cysteine peptidases

Dos Reis, Flavia C.G. and Smith, Brian O. and Santos, Camila C. and Costa, Tatiana F.R. and Scharfstein, Julio and Coombs, Graham H. and Mottram, Jeremy C. and Lima, Ana Paula C.A. (2008) The role of conserved residues of chagasin in the inhibition of cysteine peptidases. FEBS Letters, 582 (4). pp. 485-490. ISSN 0014-5793

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

We have evaluated the roles of key amino acids to the action of the natural inhibitor chagasin of papain-family cysteine peptidases. A W93A substitution decreased inhibitor affinity for human cathepsin L 100-fold, while substitutions of T31 resulted in 10-100-fold increases in the Ki for cruzipain of Trypanosoma cruzi. A T31A/T32A double mutant had increased affinity for cathepsin L but not for cruzipain, while the T31-T32 deletion drastically affected inhibition of both human and parasite peptidases. These differential effects reflect the occurrence of direct interactions between chagasin and helix 8 of cathepsin L, interactions that do not occur with cruzipain.