Related Experiment Video
Updated: Feb 2, 2026

Quantifying the Antifungal Activity of Peptides Against Candida albicans
Published on: January 13, 2023
Biochemical characterization of a Kunitz inhibitor from Inga edulis seeds with antifungal activity against Candida
Heloisa Xavier Dib1, Daniella Gorete Lourenço de Oliveira1, Caio Fernando Ramalho de Oliveira1
1Laboratório de Purificação de Proteínas e suas Funções Biológicas, Faculdade de Ciências de Alimentos e Nutrição, Universidade Federal do Mato Grosso do Sul, Campo Grande, MS, 79070-900, Brazil.
Abstract:
We describe the characterization of IETI, the first trypsin inhibitor purified from Inga edulis, a tree widely distributed in Brazil. Two-step chromatography was used to purify IETI, a protein composed of a single peptide chain of 19,685.10 Da. Amino-terminal sequencing revealed that IETI shows homology with the Kunitz family, as substantiated by its physical-chemical features, such as its thermal (up to 70 °C) and wide-range pH stability (from 2 to 10), and the value of its dissociation constant (6.2 nM). IETI contains a single reactive site for trypsin, maintained by a disulfide bridge; in the presence of DTT, its inhibitory activity was reduced in a time- and concentration-dependent manner. IETI presented activity against Candida ssp., including C. buinensis and C. tropicalis. IETI inhibitory activity triggered yeast membrane permeability, affecting cell viability, thus providing support for the use of IETI in further studies for the control of fungal infections.
Related Concept Videos
Eukaryotic Transcription Inhibitors
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
Seed Structure and Early Development of the Sporophyte
Introduction to Seed Plants
Dipeptidyl Peptidase 4 Inhibitors
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Antihypertensive Drugs: Direct Renin Inhibitors

