Trypanothione reductase inhibition and anti-leishmanial activity of all-hydrocarbon stapled α-helical peptides with improved proteolytic stability

Trypanothione reductase (TryR) is a well-established target in the search for novel antitrypanosomal and antileishmanial agents. We have previously identified linear and lactam-bridged 13-residue peptides derived from an α-helical region making up part of the dimeric interface of Leishmania infantum...

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Veröffentlicht in:	European journal of medicinal chemistry 2018-04, Vol.149, p.238-247
Hauptverfasser:	Ruiz-Santaquiteria, Marta, de Castro, Sonia, Toro, Miguel A., de Lucio, Héctor, Gutiérrez, Kilian Jesús, Sánchez-Murcia, Pedro A., Jiménez, María Ángeles, Gago, Federico, Jiménez-Ruiz, Antonio, Camarasa, María-José, Velázquez, Sonsoles
Format:	Artikel
Sprache:	eng
Schlagworte:	Antiprotozoal Agents - chemistry Cell-penetrating peptides Drug Stability Hydrocarbons - chemistry Leishmania infantum Leishmania infantum - drug effects NADH, NADPH Oxidoreductases - antagonists & inhibitors Peptides - chemistry Peptides - pharmacology Protein Conformation, alpha-Helical Protein-protein interactions Proteolysis Protozoan Proteins - antagonists & inhibitors Stapled peptides Trypanothione reductase
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