Indolicidin revisited: biological activity, potential applications and perspectives of an antimicrobial peptide not yet fully explored

ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical approaches. The antimicrobial activity assay showed that dimerization decreases the ability of the peptide to inhibit growth of bacteria or fungi; however, the dimeric analogs displayed a higher level of bactericidal activity. In addition, a dramatic increase (50 times) in hemolytic activity was achieved with these analogs. Permeabilization studies showed that the rate of carboxyfluorescein release was higher for the dimeric peptides than for the monomeric peptide, especially in vesicles that contained sphingomyelin. Despite different biological activities, the secondary structure and pore diameter were not significantly altered by dimerization. In contrast to the case for other dimeric cAMPs, we have shown that dimerization selectively decreases the antimicrobial activity of this peptide and increases the hemolytic activity. The results also show that the interaction between dimeric peptides and the cell wall could be responsible for the decrease of the antimicrobial activity of these peptides.

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Dendrimeric Sulfanyl Porphyrazines: Synthesis, Physico-Chemical Characterization, and Biological Activity for Potential Applications in Photodynamic Therapy

ChemPlusChem ◽

10.1002/cplu.201600051 ◽

2016 ◽

Vol 81 (5) ◽

pp. 460-470 ◽

Cited By ~ 21

Author(s):

Dariusz T. Mlynarczyk ◽

Sebastian Lijewski ◽

Michal Falkowski ◽

Jaroslaw Piskorz ◽

Wojciech Szczolko ◽

...

Keyword(s):

Biological Activity ◽

Photodynamic Therapy ◽

Chemical Characterization ◽

Physico Chemical ◽

Potential Applications

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Development of a Novel Biosensor Using Cationic Antimicrobial Peptide and Nickel Phthalocyanine Ultrathin Films for Electrochemical Detection of Dopamine

International Journal of Analytical Chemistry ◽

10.1155/2012/850969 ◽

2012 ◽

Vol 2012 ◽

pp. 1-7 ◽

Cited By ~ 9

Author(s):

Maysa F. Zampa ◽

Inês Maria de S. Araújo ◽

José Ribeiro dos Santos Júnior ◽

Valtencir Zucolotto ◽

José Roberto de S. A. Leite ◽

...

Keyword(s):

Antimicrobial Peptide ◽

Electrochemical Sensors ◽

Biological Fluids ◽

Fundamental Aspect ◽

Layer By Layer ◽

Cationic Antimicrobial Peptide ◽

Nickel Phthalocyanine ◽

Layer Technique ◽

Potential Applications ◽

Pharmaceutical Industries

The antimicrobial peptide dermaseptin 01 (DS 01), from the skin secretion ofPhyllomedusa hypochondrialisfrogs, was immobilized in nanostructured layered films in conjunction with nickel tetrasulfonated phthalocyanines (NiTsPc), widely used in electronic devices, using layer-by-layer technique. The films were used as a biosensor to detect the presence of dopamine (DA), a neurotransmitter associated with diseases such as Alzheimer's and Parkinson's, with detection limits in the order of 10−6 mol L−1. The use of DS 01 in LbL film generated selectivity in the detection of DA despite the presence of ascorbic acid found in biological fluids. This work is the first to report that the antimicrobial peptide and NiTsPc LbL film exhibits electroanalytical activity to DA oxidation. The selectivity in the detection of DA is a fundamental aspect for the development of electrochemical sensors with potential applications in the biomedical and pharmaceutical industries.

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Recent Advances on Triazolium Ionic Liquids: Synthesis and Applications

Current Organic Chemistry ◽

10.2174/1385272823666190627114321 ◽

2019 ◽

Vol 23 (11) ◽

pp. 1239-1255 ◽

Cited By ~ 1

Author(s):

Roli Mishra ◽

Jyoti S. Mishra ◽

Snehkrishn A. Chaubey

Keyword(s):

Ionic Liquid ◽

Biological Activity ◽

Major Part ◽

Dye Sensitized Solar Cell ◽

Storage Devices ◽

Dye Sensitized ◽

Potential Applications ◽

Electrochemical Storage ◽

Ion Conducting ◽

Hydrolysis Of

The present review is principally focused on the triazolium ILs (TILs) and its potential applications. The major part of this review deals with the use of triazolium ILs as catalysts in asymmetric synthesis, solvents, recognition abilities, and electrolytes in electrochemical, storage devices. Influences of stereochemistry in ion conducting properties, hydrolysis of sugar baggage, Dye-Sensitized Solar Cell (DSSC) and biological activity are also discussed. Our intention in this review is to make concise compilation and investigations of the latest key achievements, broad spectrum of developments and problems within triazolium ionic-liquid. We anticipate that this communication will encourage scientific researchers and industries to exploit triazolium ILs in addressing scientific accost.

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NOVEL FAMILY OF PROLINE-RICH ANTIMICROBIAL PEPTIDES INHIBITING BACTERIAL TRANSLATION

BIOTECHNOLOGY: STATE OF THE ART AND PERSPECTIVES ◽

10.37747/2312-640x-2021-19-173-174 ◽

2021 ◽

Vol 1 (19) ◽

pp. 173-174

Author(s):

R.N. Kruglikov ◽

T.V. Ovchinnikova ◽

P.V. Panteleev

Keyword(s):

Biological Activity ◽

Antimicrobial Peptides ◽

Antimicrobial Peptide ◽

Bacterial Cells ◽

Bacterial Translation

A new proline-rich antimicrobial peptide from alpaca (Vicugnia pacos) was obtained, as well as its modified analogs. The biological activity of the peptides was studied, and also the role of the N- and C-terminal fragments, when acting on bacterial cells, was analyzed.

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Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide αs2-Casein f(183–207)

Applied and Environmental Microbiology ◽

10.1128/aem.01394-13 ◽

2013 ◽

Vol 79 (17) ◽

pp. 5179-5185 ◽

Cited By ~ 18

Author(s):

Avelino Alvarez-Ordóñez ◽

Máire Begley ◽

Tanya Clifford ◽

Thérèse Deasy ◽

Kiera Considine ◽

...

Keyword(s):

Amino Acids ◽

Biological Activity ◽

Amino Acid ◽

Antimicrobial Peptide ◽

Peptide Sequence ◽

Content Type ◽

Charged Amino Acids ◽

Food Borne ◽

Relationship Of ◽

Positively Charged

ABSTRACTTemplate-based studies on antimicrobial peptide (AMP) derivatives obtained through manipulation of the amino acid sequence are helpful to identify properties or residues that are important for biological activity. The present study sheds light on the importance of specific amino acids of the milk-derived αs2-casein f(183–207) peptide to its antibacterial activity against the food-borne pathogensListeria monocytogenesandCronobacter sakazakii. Trimming of the peptide revealed that residues at the C-terminal end of the peptide are important for activity. Removal of the last 5 amino acids at the C-terminal end and replacement of the Arg at position 23 of the peptide sequence by an Ala residue significantly decreased activity. These findings suggest that Arg23 is very important for optimal activity of the peptide. Substitution of the also positively charged Lys residues at positions 15 and 17 of the αs2-casein f(183–207) peptide also caused a significant reduction of the effectiveness againstC. sakazakii, which points toward the importance of the positive charge of the peptide for its biological activity. Indeed, simultaneous replacement of various positively charged amino acids was linked to a loss of bactericidal activity. On the other hand, replacement of Pro residues at positions 14 and 20 resulted in a significantly increased antibacterial potency, and hydrophobic end tagging of αs2-casein f(193–203) and αs2-casein f(197–207) peptides with multiple Trp or Phe residues significantly increased their potency againstL. monocytogenes. Finally, the effect of pH (4.5 to 7.4), temperature (4°C to 37°C), and addition of sodium and calcium salts (1% to 3%) on the activity of the 15-amino-acid αs2-casein f(193–207) peptide was also determined, and its biological activity was shown to be completely abolished in high-saline environments.

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Shortened derivatives from native antimicrobial peptide LyeTx I: In vitro and in vivo biological activity assessment

Experimental Biology and Medicine ◽

10.1177/1535370220966963 ◽

2020 ◽

pp. 153537022096696

Author(s):

Leonardo Lima Fuscaldi ◽

Joaquim Teixeira de Avelar Júnior ◽

Daniel Moreira dos Santos ◽

Daiane Boff ◽

Vívian Louise Soares de Oliveira ◽

...

Keyword(s):

Biological Activity ◽

Antimicrobial Peptide ◽

Mammalian Cells ◽

Antimicrobial Agents ◽

Sodium Dodecyl ◽

Alpha Helix ◽

In Vitro Assays ◽

Control Group

In the continuing search for novel antibiotics, antimicrobial peptides are promising molecules, due to different mechanisms of action compared to classic antibiotics and to their selectivity for interaction with microorganism cells rather than with mammalian cells. Previously, our research group has isolated the antimicrobial peptide LyeTx I from the venom of the spider Lycosa erythrognatha. Here, we proposed to synthesize three novel shortened derivatives from LyeTx I (LyeTx I mn; LyeTx I mnΔK; LyeTx I mnΔKAc) and to evaluate their toxicity and biological activity as potential antimicrobial agents. Peptides were synthetized by Fmoc strategy and circular dichroism analysis was performed, showing that the three novel shortened derivatives may present membranolytic activity, like the original LyeTx I, once they folded as an alpha helix in 2.2.2-trifluorethanol and sodium dodecyl sulfate. In vitro assays revealed that the shortened derivative LyeTx I mnΔK presents the best score between antimicrobial (↓ MIC) and hemolytic (↑ EC50) activities among the synthetized shortened derivatives, and LUHMES cell-based NeuriTox test showed that it is less neurotoxic than the original LyeTx I (EC50 [LyeTx I mnΔK] ⋙ EC50 [LyeTx I]). In vivo data, obtained in a mouse model of septic arthritis induced by Staphylococcus aureus, showed that LyeTx I mnΔK is able to reduce infection, as demonstrated by bacterial recovery assay (∼10-fold reduction) and scintigraphic imaging (less technetium-99m labeled-Ceftizoxime uptake by infectious site). Infection reduction led to inflammatory process and pain decreases, as shown by immune cells recruitment reduction and threshold nociception increment, when compared to positive control group. Therefore, among the three shortened peptide derivatives, LyeTx I mnΔK is the best candidate as antimicrobial agent, due to its smaller amino acid sequence and toxicity, and its greater biological activity.

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