Picture of athlete cycling

Open Access research with a real impact on health...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the Physical Activity for Health Group based within the School of Psychological Sciences & Health. Research here seeks to better understand how and why physical activity improves health, gain a better understanding of the amount, intensity, and type of physical activity needed for health benefits, and evaluate the effect of interventions to promote physical activity.

Explore open research content by Physical Activity for Health...

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.