The emergence of antibiotic-resistant microbes has stimulated research
worldwide seeking new biologically active molecules. In this respect,
synthetic antimicrobial peptides (SAMPs) have been suggested to overcome
this problem. Although there are some online servers that provide
putative SAMPs from protein sequences, the choice of the best peptide
sequences for further analysis is still difficult. Therefore, the goal
of this paper is not to launch a new tool but to provide a friendly
workflow to characterize and predict potential SAMPs by employing
existing tools. Using this proposed workflow, two peptides (PepGAT and
PepKAA) were obtained and extensively characterized. These peptides
damaged microbial membranes and cell walls, and induced overproduction
of reactive oxygen species (ROS). Both peptides were found to assume
random coil secondary structure in aqueous solution, organic solvent,
and upon binding to negatively charged lipid systems. Peptides were also
able to degrade formed biofilms but not to prevent biofilm formation.
PepGAT was not resistant to proteolysis, whereas PepKAA was resistant to
pepsin but not to pancreatin. Furthermore, both presented no hemolytic
activity against red blood cells, even at a 10-fold higher concentration
than the antimicrobial concentration. The pipeline proposed here is an
easy way to design new SAMPs for application as alternatives to develop
new drugs against human pathogenic microorganisms. (C) 2020 Elsevier
B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM).
All rights reserved.
%0 Journal Article
%1 WOS:000579382300015
%A Souza, Pedro F N
%A Marques, Lidyane S M
%A Oliveira, Jose T A
%A Lima, Patricia G
%A Dias, Lucas P
%A Neto, Nilton A S
%A Lopes, Francisco E S
%A Sousa, Jeanlex S
%A Silva, Ayrles F B
%A Caneiro, Romulo F
%A Lopes, Jose L S
%A V, Marcio Ramos
%A Freitas, Cleverson D T
%C 65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE
%D 2020
%I ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
%J BIOCHIMIE
%K Candida; Dermatophyte; Peptide SAMP} activity; design; {Antibiofilm
%P 132-145
%R 10.1016/j.biochi.2020.05.016
%T Synthetic antimicrobial peptides: From choice of the best sequences to
action mechanisms
%V 175
%X The emergence of antibiotic-resistant microbes has stimulated research
worldwide seeking new biologically active molecules. In this respect,
synthetic antimicrobial peptides (SAMPs) have been suggested to overcome
this problem. Although there are some online servers that provide
putative SAMPs from protein sequences, the choice of the best peptide
sequences for further analysis is still difficult. Therefore, the goal
of this paper is not to launch a new tool but to provide a friendly
workflow to characterize and predict potential SAMPs by employing
existing tools. Using this proposed workflow, two peptides (PepGAT and
PepKAA) were obtained and extensively characterized. These peptides
damaged microbial membranes and cell walls, and induced overproduction
of reactive oxygen species (ROS). Both peptides were found to assume
random coil secondary structure in aqueous solution, organic solvent,
and upon binding to negatively charged lipid systems. Peptides were also
able to degrade formed biofilms but not to prevent biofilm formation.
PepGAT was not resistant to proteolysis, whereas PepKAA was resistant to
pepsin but not to pancreatin. Furthermore, both presented no hemolytic
activity against red blood cells, even at a 10-fold higher concentration
than the antimicrobial concentration. The pipeline proposed here is an
easy way to design new SAMPs for application as alternatives to develop
new drugs against human pathogenic microorganisms. (C) 2020 Elsevier
B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM).
All rights reserved.
@article{WOS:000579382300015,
abstract = {The emergence of antibiotic-resistant microbes has stimulated research
worldwide seeking new biologically active molecules. In this respect,
synthetic antimicrobial peptides (SAMPs) have been suggested to overcome
this problem. Although there are some online servers that provide
putative SAMPs from protein sequences, the choice of the best peptide
sequences for further analysis is still difficult. Therefore, the goal
of this paper is not to launch a new tool but to provide a friendly
workflow to characterize and predict potential SAMPs by employing
existing tools. Using this proposed workflow, two peptides (PepGAT and
PepKAA) were obtained and extensively characterized. These peptides
damaged microbial membranes and cell walls, and induced overproduction
of reactive oxygen species (ROS). Both peptides were found to assume
random coil secondary structure in aqueous solution, organic solvent,
and upon binding to negatively charged lipid systems. Peptides were also
able to degrade formed biofilms but not to prevent biofilm formation.
PepGAT was not resistant to proteolysis, whereas PepKAA was resistant to
pepsin but not to pancreatin. Furthermore, both presented no hemolytic
activity against red blood cells, even at a 10-fold higher concentration
than the antimicrobial concentration. The pipeline proposed here is an
easy way to design new SAMPs for application as alternatives to develop
new drugs against human pathogenic microorganisms. (C) 2020 Elsevier
B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM).
All rights reserved.},
added-at = {2022-05-23T20:00:14.000+0200},
address = {65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE},
author = {Souza, Pedro F N and Marques, Lidyane S M and Oliveira, Jose T A and Lima, Patricia G and Dias, Lucas P and Neto, Nilton A S and Lopes, Francisco E S and Sousa, Jeanlex S and Silva, Ayrles F B and Caneiro, Romulo F and Lopes, Jose L S and V, Marcio Ramos and Freitas, Cleverson D T},
biburl = {https://www.bibsonomy.org/bibtex/277fd8d1caddc2cc92afd54f456eb9b49/ppgfis_ufc_br},
doi = {10.1016/j.biochi.2020.05.016},
interhash = {d80a7859d4f30175c94cdea3d888ec66},
intrahash = {77fd8d1caddc2cc92afd54f456eb9b49},
issn = {0300-9084},
journal = {BIOCHIMIE},
keywords = {Candida; Dermatophyte; Peptide SAMP} activity; design; {Antibiofilm},
pages = {132-145},
publisher = {ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER},
pubstate = {published},
timestamp = {2022-05-23T20:00:14.000+0200},
title = {Synthetic antimicrobial peptides: From choice of the best sequences to
action mechanisms},
tppubtype = {article},
volume = 175,
year = 2020
}