Synthetic antimicrobial peptides: Characteristics, design, and potential as alternative molecules to overcome microbial resistance

Life Sciences ◽  
2021 ◽  
pp. 119647
Author(s):  
Patrícia G. Lima ◽  
Jose T.A. Oliveira ◽  
Jackson L. Amaral ◽  
Cleverson D.T. Freitas ◽  
Pedro F.N. Souza
Keyword(s):  
Antimicrobial Peptides ◽  
Microbial Resistance ◽  
Synthetic Antimicrobial Peptides

Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides

2018 ◽  
Vol 26 (6) ◽  
pp. 1189-1196 ◽  
Author(s):  
Tracy A. Stone ◽  
Gregory B. Cole ◽  
Huong Q. Nguyen ◽  
Simon Sharpe ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Interactions ◽  
Synthetic Antimicrobial Peptides

scholarly journals Interaction of synthetic antimicrobial peptides of the Hylin a1 family with models of eukaryotic structures: Zwitterionic membranes and DNA

2020 ◽  
Vol 24 ◽  
pp. 100827
Author(s):  
Gabriel S. Vignoli Muniz ◽  
Lilia I. De la Torre ◽  
Evandro L. Duarte ◽  
Esteban N. Lorenzón ◽  
Eduardo M. Cilli ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Synthetic Antimicrobial Peptides

scholarly journals Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae

2014 ◽  
Vol 2014 ◽  
pp. 1-13 ◽  
Author(s):  
Hanbo Chai ◽  
William E. Allen ◽  
Rickey P. Hicks
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Klebsiella Pneumoniae ◽  
Antimicrobial Peptides ◽  
Inhibitory Activity ◽  
Binding Conformation ◽  
Cd Studies ◽  
Synthetic Antimicrobial Peptides ◽  
Activity Mechanism ◽  
Binding Mechanisms

Circular dichroism and 1H NMR were used to investigate the interactions of a series of synthetic antimicrobial peptides (AMPs) with lipopolysaccharides (LPS) isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae. Previous CD studies with AMPs containing only three Tic-Oic dipeptide units do not exhibit helical characteristics upon interacting with small unilamellar vesicles (SUVs) consisting of LPS. Increasing the number of Tic-Oic dipeptide units to six resulted in five analogues with CD spectra that exhibited helical characteristics on binding to LPS SUVs. Spectroscopic and in vitro inhibitory data suggest that there are two possible helical conformations resulting from two different AMP-LPS binding mechanisms. Mechanism one involves a helical binding conformation where the AMP binds LPS very strongly and is not efficiently transported across the LPS bilayer resulting in the loss of inhibitory activity. Mechanism two involves a helical binding conformation where the AMP binds LPS very loosely and is efficiently transported across the LPS bilayer resulting in an increase in inhibitory activity. Mechanism three involves a nonhelical binding conformation where the AMP binds LPS very loosely and is efficiently transported across the LPS bilayer resulting in an increase in inhibitory activity.

Design of Synthetic Antimicrobial Peptides Based on Sequence Analogy and Amphipathicity

1997 ◽  
Vol 250 (2) ◽  
pp. 549-558 ◽  
Author(s):  
Alessandro Tossi ◽  
Chiara Tarantino ◽  
Domenico Romeo
Keyword(s):  
Antimicrobial Peptides ◽  
Synthetic Antimicrobial Peptides

scholarly journals Synthetic Antimicrobial Peptides: III—Effect of Cationic Groups of Lysine, Arginine, and Histidine on Antimicrobial Activity of Peptides with a Linear Type of Amphipathicity

2021 ◽  
Vol 47 (3) ◽  
pp. 681-690
Author(s):  
N. V. Amirkhanov ◽  
A. V. Bardasheva ◽  
N. V. Tikunova ◽  
D. V. Pyshnyi
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity ◽  
Antibacterial Properties ◽  
Bacterial Cells ◽  
Pathogenic Yeast ◽  
Linear Type ◽  
Histidine Residues ◽  
Cationic Amino Acid ◽  
Arginine Residues ◽  
Synthetic Antimicrobial Peptides

Abstract We have studied the antimicrobial and hemolytic activity of synthetic antimicrobial peptides (SAMPs), i.e., Arg9Phe2 (P1-Arg), Lys9Phe2 (P2-Lys), and His9Phe2 (P3-His), which have a “linear” type of amphipathicity and contain the cationic amino acid residues of arginine, lysine, or histidine. In this study, we have used various pathogenic microorganism strains of gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli, and Salmonella enterica), gram-positive bacteria (Staphylococcus aureus), and the conditionally pathogenic yeast fungus (Candida albicans). It has been shown that the replacement of the arginine residues by lysine or histidine residues in the tested SAMPs significantly degrades their antibacterial properties in the series: P1-Arg > P2-Lys $$ \gg $$P3-His. The cationic analog of SAMP, P1-Arg, has the highest antibacterial activity (MIC50 = 43–76 μM), while peptide P3-His does not exhibit this activity (MIC50 > 100 μM). The P1-Arg and P2-Lys peptides were 6–10 times more active against the opportunistic fungus C. albicans (MIC50 6.7 and 10.9 μM, respectively) and the P3-His peptide has 100-times increased antimycotic activity (MIC50 0.6 μM) compared with their effect on bacterial cells. All of the tested peptides with the linear type of amphipathicity and low hydrophobicity, i.e., P1-Arg, P2-Lys, and P3-His, that contain only two Phe residues regardless of the presence of cationic amino acids (Arg, Lys, or His) exhibit a relatively low hemolytic activity (not more than 4% hemolysis at 1000 μM peptide concentration). Thus, considering the same synthesis efficiency (56–63%) and approximately the same low toxicity of the tested SAMPs with a linear type of amphipathicity, it is recommended to use those that contain the cationic arginine or histidine residues to create antibacterial or antifungal peptide agents, respectively.

scholarly journals Activity of Genital Tract Secretions and Synthetic Antimicrobial Peptides against Group BStreptococcus

2015 ◽  
Vol 74 (6) ◽  
pp. 499-507
Author(s):  
Nidhi Agarwal ◽  
Niall Buckley ◽  
Natasha Nakra ◽  
Philip Gialanella ◽  
Weirong Yuan ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Genital Tract ◽  
Synthetic Antimicrobial Peptides

Cell Penetrating Synthetic Antimicrobial Peptides (SAMPs) Exhibiting Potent and Selective Killing ofMycobacteriumby Targeting Its DNA

2015 ◽  
Vol 21 (9) ◽  
pp. 3540-3545 ◽  
Author(s):  
Aashish Sharma ◽  
Amol Arunrao Pohane ◽  
Sandhya Bansal ◽  
Avinash Bajaj ◽  
Vikas Jain ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Penetrating ◽  
Synthetic Antimicrobial Peptides
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