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

Flavia C.G. Dos Reis, Brian O. Smith, Camila C. Santos, Tatiana F.R. Costa, Julio Scharfstein, Graham H. Coombs, Jeremy C. Mottram, Ana Paula C.A. Lima

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)485-490
Number of pages5
JournalFEBS Letters
Issue number4
Publication statusPublished - 20 Feb 2008


  • chagasin
  • cysteine peptidase
  • inhibitor
  • mutant
  • Trypanosoma


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