Analysis of Structure and Hemolytic Activity Relationships of Antimicrobial Peptides (AMPs)

2014 ◽  
pp. 253-258 ◽  
Author(s):  
Jennifer Ruiz ◽  
Jhon Calderon ◽  
Paola Rondón-Villarreal ◽  
Rodrigo Torres
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity

Synergy of action of antimicrobial peptides PG-1 and ChBac3.4 with antiseptics against antibiotic-resistant bacteria

2018 ◽  
Vol 18 (4) ◽  
pp. 47-57
Author(s):  
Maria Sergeyevna Zharkova ◽  
Ekaterina S. Umnyakova ◽  
Anna G. Afinogenova ◽  
Gennady E. Afinogenov ◽  
Aleksandr A. Kolobov ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Sodium Hypochlorite ◽  
Hemolytic Activity ◽  
Etidronic Acid ◽  
Resistant Bacteria ◽  
Bacterial Cells ◽  
Antibiotic Resistant Bacteria ◽  
Antibiotic Resistant ◽  
Bacterial Membranes ◽  
Combined Action

We investigated the combined effects of antimicrobial peptides PG-1 and ChBac3.4 with antiseptics (sodium hypochlorite, dioxidine, prontosan, poviargolum, and etidronic acid) to identify combinations that display synergistic antimicrobial activity against antibiotic-resistant bacteria. We used the checker-board titration method to calculate fractional inhibitory concentration indices, and based on the indices the type of combined action was determined. The combined effect on the metabolic activity of bacteria was evaluated using the fluorescent marker resazurin, and the effect on the permeability of bacterial membranes for chromogenic markers was studied spectrophotometrically. The combined hemolytic activity of the combinations was investigated. Sodium hypochlorite was shown to be antagonistic with both antimicrobial peptides. With other antiseptics, combined action was characterized by additivity or synergy. Synergy was most pronounced with the preparation of highly dispersed silver poviargolum. Antiseptics accelerate the development of the antimicrobial effect of antimicrobial peptides but do not significantly affect the dynamics of the membranolytic action of antimicrobial peptides on bacterial cells. Synergy of hemolytic activity is rare. Thus, the combined use of antimicrobial peptides and antiseptics is promising for combating antibiotic-resistant bacteria and can be used to reduce the toxic effects of these compounds.

scholarly journals Lipid selectivity in novel antimicrobial peptides: Implication on antimicrobial and hemolytic activity

2017 ◽  
Vol 153 ◽  
pp. 152-159 ◽  
Author(s):  
P. Maturana ◽  
M. Martinez ◽  
M.E. Noguera ◽  
N.C. Santos ◽  
E.A. Disalvo ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity

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 Can Peptide-Lipid Interactions Predict Bactericidal and Hemolytic Activity in Antimicrobial Peptides?

2009 ◽  
Vol 96 (3) ◽  
pp. 155a
Author(s):  
Jing He ◽  
Michelle Pate ◽  
Janet Hammer ◽  
Jack Blazyk
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity ◽  
Lipid Interactions

Structure-function relationships of antimicrobial peptides

1998 ◽  
Vol 76 (2-3) ◽  
pp. 235-246 ◽  
Author(s):  
Peter M Hwang ◽  
Hans J Vogel
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity ◽  
Mammalian Cells ◽  
Rational Design ◽  
Current Knowledge ◽  
Membrane Binding ◽  
Three Dimensional ◽  
Exact Nature ◽  
Additional Information ◽  
Bacteria And Fungi

Antimicrobial peptides are ubiquitously produced throughout nature. Many of these relatively short peptides (6-50 residues) are lethal towards bacteria and fungi, yet they display minimal toxicity towards mammalian cells. All of the peptides are highly cationic and hydrophobic. It is widely believed that they act through nonspecific binding to biological membranes, even though the exact nature of these interactions is presently unclear. High-resolution nuclear magnetic resonance (NMR) has contributed greatly to knowledge in this field, providing insight about peptide structure in aqueous solution, in organic cosolvents, and in micellar systems. Solid-state NMR can provide additional information about peptide-membrane binding. Here we review our current knowledge about the structure of antimicrobial peptides. We also discuss studies pertaining to the mechanism of action. Despite the different three-dimensional structural motifs of the various classes, they all have similar amphiphilic surfaces that are well-suited for membrane binding. Many antimicrobial peptides bind in a membrane-parallel orientation, interacting only with one face of the bilayer. This may be sufficient for antimicrobial action. At higher concentrations, peptides and phospholipids translocate to form multimeric transmembrane channels that seem to contribute to the peptide's hemolytic activity. An understanding of the key features of the secondary and tertiary structures of the antimicrobial peptides and their effects on bactericidal and hemolytic activity can aid the rational design of improved analogs for clinical use.Key words: structure, antimicrobial peptide, NMR, membrane, hemolytic.

scholarly journals Silver Nanoparticles Functionalized With Antimicrobial Polypeptides: Benefits and Possible Pitfalls of a Novel Anti-infective Tool

2021 ◽  
Vol 12 ◽  
Author(s):  
Maria S. Zharkova ◽  
Olga Yu. Golubeva ◽  
Dmitriy S. Orlov ◽  
Elizaveta V. Vladimirova ◽  
Alexander V. Dmitriev ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Tumor Cells ◽  
Hemolytic Activity ◽  
Dermal Fibroblasts ◽  
Host Cells ◽  
Eukaryotic Cells ◽  
Drug Resistant ◽  
Antimicrobial Polypeptides

Silver nanoparticles (AgNPs) and antimicrobial peptides or proteins (AMPs/APs) are both considered as promising platforms for the development of novel therapeutic agents effective against the growing number of drug-resistant pathogens. The observed synergy of their antibacterial activity suggested the prospect of introducing antimicrobial peptides or small antimicrobial proteins into the gelatinized coating of AgNPs. Conjugates with protegrin-1, indolicidin, protamine, histones, and lysozyme were comparatively tested for their antibacterial properties and compared with unconjugated nanoparticles and antimicrobial polypeptides alone. Their toxic effects were similarly tested against both normal eukaryotic cells (human erythrocytes, peripheral blood mononuclear cells, neutrophils, and dermal fibroblasts) and tumor cells (human erythromyeloid leukemia K562 and human histiocytic lymphoma U937 cell lines). The AMPs/APs retained their ability to enhance the antibacterial activity of AgNPs against both Gram-positive and Gram-negative bacteria, including drug-resistant strains, when conjugated to the AgNP surface. The small, membranolytic protegrin-1 was the most efficient, suggesting that a short, rigid structure is not a limiting factor despite the constraints imposed by binding to the nanoparticle. Some of the conjugated AMPs/APs clearly affected the ability of nanoparticle to permeabilize the outer membrane of Escherichia coli, but none of the conjugated AgNPs acquired the capacity to permeabilize its cytoplasmic membrane, regardless of the membranolytic potency of the bound polypeptide. Low hemolytic activity was also found for all AgNP-AMP/AP conjugates, regardless of the hemolytic activity of the free polypeptides, making conjugation a promising strategy not only to enhance their antimicrobial potential but also to effectively reduce the toxicity of membranolytic AMPs. The observation that metabolic processes and O2 consumption in bacteria were efficiently inhibited by all forms of AgNPs is the most likely explanation for their rapid and bactericidal action. AMP-dependent properties in the activity pattern of various conjugates toward eukaryotic cells suggest that immunomodulatory, wound-healing, and other effects of the polypeptides are at least partially transferred to the nanoparticles, so that functionalization of AgNPs may have effects beyond just modulation of direct antibacterial activity. In addition, some conjugated nanoparticles are selectively toxic to tumor cells. However, caution is required as not all modulatory effects are necessarily beneficial to normal host cells.

Design of cyclic antimicrobial peptides with low hemolytic activity

2006 ◽  
pp. 88-91
Author(s):  
L. H. Kondejewski ◽  
M. Jelokhani-Niaraki ◽  
E. J. Prenner ◽  
R. N. A. H. Lewis ◽  
R. N. McElhaney ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity

NOVEL β-HAIRPIN ANTIMICROBIAL PEPTIDES FROM MARINE POLYCHAETA

2020 ◽  
pp. 209-210
Author(s):  
P. Panteleev ◽  
I. Bolosov ◽  
S. Sychev ◽  
T. Ovchinnikova
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity ◽  
Arenicola Marina ◽  
Capitella Teleta

Recombinant β-hairpin BRICHOS-associated antimicrobial peptides from the polychaetes Capitella teleta and Arenicola marina were obtained, and their antibacterial and hemolytic activity was studied.

Sign in / Sign up

Export Citation Format

Share Document