Journal
PHARMACEUTICALS
Volume 14, Issue 7, Pages -Publisher
MDPI
DOI: 10.3390/ph14070689
Keywords
leishmaniasis; small molecule-peptide conjugates; dimerization inhibitors; trypanothione disulfide reductase
Categories
Funding
- Spanish MICINN [PID2019-104070RB-C21, PID2019-104070RB-C22]
- Spanish Agencia Estatal Consejo Superior de Investigaciones Cientificas (CSIC) [CSIC-PIE-201980E100, CSIC-PIE-201980E028]
- Comunidad de Madrid [PLATESA2-CM, S-2018/BAA-4370]
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By disrupting protein-protein interactions at the dimer interface of Leishmania infantum TryR, researchers have developed a novel series of small-molecule-peptide conjugates that show good inhibitory effects on both enzyme activity and dimerization.
Trypanothione disulfide reductase (TryR) is an essential homodimeric enzyme of trypanosomatid parasites that has been validated as a drug target to fight human infections. Using peptides and peptidomimetics, we previously obtained proof of concept that disrupting protein-protein interactions at the dimer interface of Leishmania infantum TryR (LiTryR) offered an innovative and so far unexploited opportunity for the development of novel antileishmanial agents. Now, we show that linking our previous peptide prototype TRL38 to selected hydrophobic moieties provides a novel series of small-molecule-peptide conjugates that behave as good inhibitors of both LiTryR activity and dimerization.
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