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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.

Authors :
Dias LP
Souza PFN
Oliveira JTA
Vasconcelos IM
Araújo NMS
Tilburg MFV
Guedes MIF
Carneiro RF
Lopes JLS
Sousa DOB
Source :
Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2020 Feb 01; Vol. 1862 (2), pp. 183092. Date of Electronic Publication: 2019 Oct 31.
Publication Year :
2020

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.<br /> (Copyright © 2019 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1879-2642
Volume :
1862
Issue :
2
Database :
MEDLINE
Journal :
Biochimica et biophysica acta. Biomembranes
Publication Type :
Academic Journal
Accession number :
31678367
Full Text :
https://doi.org/10.1016/j.bbamem.2019.183092