| Full text | |
| Author(s): |
Souza, Larissa A. L.
;
Dias, Lucas P.
;
Araujo, Nadine M. S.
;
Carneiro, Romulo F.
;
Nagano, Celso S.
;
Teixeira, Claudener S.
;
Silva, Rafael G. G.
;
Oliveira, Jose T. A.
;
Sousa, Daniele O. B.
Total Authors: 9
|
| Document type: | Journal article |
| Source: | Biochimie; v. 200, p. 12-pg., 2022-09-01. |
| Abstract | |
Antimicrobial resistance has been increasing globally, posing a global public health risk. It has prompted the scientific community to look for alternatives to traditional drugs. Antimicrobial Peptides (AMPs) have stood out in this context because they have the potential to control infectious diseases while causing no or little harm to mammalian cells. In the present study, three peptides, JcTI-PepI, JcTI-PepII, and JcTI-PepIII, were designed and tested for antimicrobial activity based on the primary sequence of JcTI-I, a 2S albumin with trypsin inhibitory activity from Jatropha curcas. JcTI-PepI strongly inhibited C. krusei growth, and it caused severe disruptions in cellular processes and cell morphology. C. krusei cells treated with JcTI-PepI showed indicative of membrane permeabilization and overproduction of Reactive Oxygen Species. Moreover, the yeast's ability to acidify the medium was severely compromised. JcTI-PepI was also effective against pre-formed biofilm and did not harm human erythrocytes and Vero cells. Overall, these characteristics indicate that JcTI-PepI is both safe and effective against C. krusei, an intrinsically resistant strain that causes serious health problems and is frequently overlooked. It implies that this peptide has a high potential for use as a new antimicrobial agent in the future. (c) 2022 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU) | |
| FAPESP's process: | 20/03998-6 - Effect of the interaction of antimicrobial peptides on the structuring of the lipid bilayer |
| Grantee: | Lucas Pinheiro Dias |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |