Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

RcAlb-PepII, a synthetic small peptide bioinspired in the 2S albumin from the seed cake of Ricinus communis, is a potent antimicrobial agent against Klebsiella pneumoniae and Candida parapsilosis

Full text
Author(s):
Dias, Lucas P. [1] ; Souza, Pedro F. N. [1] ; Oliveir, Jose T. A. [1] ; Vasconcelos, Ilka M. [1] ; Araujo, Nadine M. S. [1] ; Tilburg, Mauricio F. V. [2] ; Guedes, Maria I. F. [2] ; Carneiro, Romulo F. [3] ; Lopes, Jose L. S. [4] ; Sousa, Daniele O. B. [1]
Total Authors: 10
Affiliation:
[1] Fed Univ Ceara UFC, Dept Biochem & Mol Biol, Fortaleza, Ceara - Brazil
[2] State Univ Ceara UECE, Dept Biotechnol, Fortaleza, Ceara - Brazil
[3] Fed Univ Ceara UFC, Dept Fisheries Engn, Fortaleza, Ceara - Brazil
[4] Univ Sao Paulo IF USP, Dept Appl Phys, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES; v. 1862, n. 2 FEB 1 2020.
Web of Science Citations: 0
Abstract

Antimicrobial peptides (AMPs) are important constituents of the innate immunity system of all living organisms. They participate in the first line of defense against invading pathogens such as viruses, bacteria, and fungi. In view of the increasing difficulties to treat infectious diseases due to the emergence of antibiotic-resistant bacterial strains, AMPs have great potential to control infectious diseases in humans and animals. In this study, two small peptides, RcAlb-PepI and RcAlb-PepII, were designed based on the primary structure of Rc-2S-Alb, a 2S albumin from the seed cake of Ricinus communis, and their antimicrobial activity assessed. RcAlb-PepII strongly inhibited the growth of Klebsiella pneumoniae and Candida parapsilosis, and induced morphological alterations in their cell surface. C. parapsilosis exposed to RcAlb-PepII presented higher cell membrane permeabilization and elevated content of reactive oxygen species. RcAlb-PepII also degraded and reduced the biofilm formation in C. parapsilosis and in K. pneumonia cells. Experimentally, RcAlb-PepII was not hemolytic and had low toxicity to mammalian cells. These are advantageous characteristics, which suggest that RcAlb-PepII is safe and apparently effective for its intended use and has great potential for the future development of an antimicrobial agent with the ability to kill or inhibit K. pneumoniae and C. parapsilosis cells. (AU)

FAPESP's process: 18/19546-7 - Molecular mechanisms of the binding, insertion, and orientation of antimicrobial peptides in model membranes
Grantee:Jose Luiz de Souza Lopes
Support Opportunities: Regular Research Grants