Fast and potent bactericidal membrane lytic activity of PaDBS1R1, a novel cationic antimicrobial peptide

Irazazabal, Luz N.; Porto, William F.; Fensterseifer, Isabel C. M.; Alves, E.S.F.; Matos, Carolina O.; Menezes, Antônio Carlos Severo; Felício, Mário R.; Gonçalves, Sónia; Santos, Nuno C.; Ribeiro, Suzana Meira; Humblot, Vincent; Lião, Luciano M.; Ladram, Ali; Franco, Octávio Luiz

doi:10.1016/j.bbamem.2018.08.001

Cited by 41 publications

(27 citation statements)

References 74 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…From this sequence (by inserting the α-helical pattern described above), the variants PaDBS1R1 and PaDBS1R6 were generated. PaDBS1R1 displayed potent antibacterial activity, with low micromolar MIC values ranging from 1.5 to 12.5 µM against Gram-negative and Grampositive bacteria (Table 2) (Irazazabal et al, 2019). Moreover, the PaDBS1R6 peptide, which was also tested against Gramnegative and Gram-positive bacteria of clinical interest, proved to be selective for Gram-negative strains ( Table 2).…”

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

et al. 2020

View full text Add to dashboard Cite

Computer-Aided Design of Antimicrobial Peptides http://crdd.osdd.net/raghava/antibp2/ ClassAMP Uses RF and SVM to predict the propensity of a protein sequence to have antibacterial, antifungal, or antiviral activity http://www.bicnirrh.res.in/classamp/ AMPA Web tool for assessing the antimicrobial domains of proteins, with a focus on the design on new antimicrobial drugs http://tcoffee.crg.cat/apps/ampa/do DBAASP Provides users with information on detailed structure (chemical, 3D) and activity for those peptides, for which antimicrobial activity against particular target species have been evaluated experimentally https://dbaasp.org/home Joker An algorithm to design antimicrobial peptides using their language https://github.com/williamfp7/Joker

show abstract

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

et al. 2020

View full text Add to dashboard Cite

show abstract

“…However, as new peptides were tested, an ability to kill Gram-positive bacteria could be observed, e.g. for PaDBS1R1 (11) and EcDBS1R5 (12). EcDBS1R6 (18) is also capable of killing Gram-positive bacteria, in addition to Gram-negatives (Table 1).…”

Section: Discussionmentioning

confidence: 99%

“…Joker provides an algorithm that is an initial step in developing novel AMPs and 84 sequences were screened in our initial study. Now we have started the second step of characterizing the lead peptides (11, 12).…”

Section: Introductionmentioning

confidence: 99%

EcDBS1R6: A new broad-spectrum cationic antibacterial peptide derived from a signal peptide sequence

Porto

Irazazabal²,

Humblot

et al. 2019

Preprint

Self Cite

View full text Add to dashboard Cite

Bacterial infections represent a major worldwide health problem, with an special highlight on Gram-negative bacteria, which were assigned by the World Health Organization (WHO) as the most critical priority for development of novel antimicrobial compounds. Antimicrobial peptides (AMPs) have been considered as potential alternative agents for treating these infections. Here we demonstrated the broad-spectrum activity of EcDBS1R6, a peptide derived from a signal peptide sequence of Escherichia coli that we previously turned into an AMP by making changes predicted through the Joker algorithm.Signal peptides are known to naturally interact with membranes; however, the modifications introduced by Joker made this peptide capable of killing bacteria. Membrane damage of the bacterial cells was observed by measuring membrane integrity using fluorescent probes and through scanning electron microscopy imaging. Structural analysis revealed that the C-terminus was unable to fold into an α -helix, indicating that the EcDBS1R6 antibacterial activity core was located at the N-terminus, corresponding to the signal peptide portion of the parent peptide. Therefore, the strategy of transforming signal peptides into AMPs seems to be promising and could be used for producing novel antimicrobial agents.

show abstract

“…Besides, the rapid antimicrobial action of AMPs was also widely known [ [25] , [26] , [27] ]. For examples, an antimicrobial peptide mBjAMP1 can completely kill the Gram-positive bacteria Staphylococcus aureus ( S. aureus ) within 30 min and the Gram-negative bacteria Escherichia coli ( E. coli ) within 3 h [ 28 ]; Another antimicrobial peptide PaDBS1R1 at 6.25 μM even kill all of the S. aureus after 30 min and E. coli after 5 min [ 29 ]; In a more extensive investigation, an antimicrobial peptide isolated from chicken (CHAP) exhibited potent and fast activity against 19 strains of bacteria including drug-resistant strains as CHAP showed 50–94% of its inhibition activity to almost all the tested bacteria species after only 30 min [ 30 ].…”

Section: Amps As Alternative Of Conventional Antibiotics For Infectiomentioning

confidence: 99%

Antimicrobial peptides – Advances in development of therapeutic applications

2020

View full text Add to dashboard Cite

The severe infection is becoming a significant health problem which threaten the lives of patients and the safety and economy of society. In the way of finding new strategy, antimicrobial peptides (AMPs) - an important part of host defense family, emerged with tremendous potential. Up to date, huge numbers of AMPs has been investigated from both natural and synthetic sources showing not only the ability to kill microbial pathogens but also propose other benefits such as wound healing, anti-tumor, immune modulation. In this review, we describe the involvements of AMPs in biological systems and discuss the opportunity in developing AMPs for clinical applications. In the detail, their properties in antibacterial activity is followed by their application in some infection diseases and cancer. The key discussions are the approaches to improve biological activities of AMPs either by modifying chemical structure or incorporating into delivery systems. The new applications and perspectives for the future of AMPs would open the new era of their development.

show abstract

Fast and potent bactericidal membrane lytic activity of PaDBS1R1, a novel cationic antimicrobial peptide

Cited by 41 publications

References 74 publications

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

EcDBS1R6: A new broad-spectrum cationic antibacterial peptide derived from a signal peptide sequence

Antimicrobial peptides – Advances in development of therapeutic applications

Contact Info

Product

Resources

About