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Updated: Jul 1, 2025
Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Design and Evaluation of a Novel Anti-microbial Peptide from Cathelicidin-2: Selectively Active Against Acinetobacter
Fariba Fathi1, Maryam Ghobeh1, Farshad H Shirazi2,3
1Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Background:
Infections caused by pathogenic microorganisms have increased the need for hospital care and have thus represented a public health problem and a significant financial burden. Classical treatments consisting of traditional antibiotics face several challenges today. Anti-microbial peptides (AMPs) are a conserved characteristic of the innate immune response among different animal species to defend against pathogenic microorganisms.
Objectives:
In this study, a new peptide sequence (mCHTL131-140) was designed using the in silico approach.
Methods:
Cathelicidin-2 (UniprotID: Q2IAL7) was used as a potential antimicrobial protein, and a novel 10 - 12 amino acids sequence AMP was designed using bioinformatics tools and the AMP databases. Then, the anti-bacterial, anti-biofilm, and anti-fungal properties of the peptide, as well as its hemolytic activity and cytotoxicity towards human fibroblast (HDF) cells, were investigated in vitro.
Results:
Online bioinformatics tools indicated that the peptide sequence could have anti-bacterial, anti-viral, anti-fungal, and anti-biofilm properties with little hemolytic properties. The experimental tests confirmed that mCHTL131-140 exhibited the best anti-bacterial properties against Acinetobacter baumannii and had fair anti-fungal properties. Besides, it did not cause red blood cell lysis and showed no cytotoxicity towards HDF cells.
Conclusions:
In general, the designed peptide can be considered a promising AMP to control hospital-acquired infections by A. baumannii.
Insights
A novel antimicrobial peptide (AMP) was designed using bioinformatics to combat drug-resistant bacteria. This peptide showed strong antibacterial activity against Acinetobacter baumannii and was non-toxic, offering a potential solution for hospital-acquired infections.
Area of Science:
- Biotechnology
- Infectious Diseases
- Drug Discovery
Background:
- Rising antimicrobial resistance necessitates novel therapeutic strategies.
- Antimicrobial peptides (AMPs) are a crucial component of the innate immune system.
- Traditional antibiotics face increasing challenges in treating microbial infections.
Purpose of the Study:
- To design and evaluate a novel antimicrobial peptide (AMP) sequence, mCHTL131-140.
- To assess the in vitro antibacterial, antifungal, and anti-biofilm properties of the designed peptide.
- To investigate the hemolytic activity and cytotoxicity of the peptide against human cells.
Main Methods:
- In silico design of a 10-12 amino acid peptide sequence based on Cathelicidin-2.
- Bioinformatic analysis to predict antimicrobial and hemolytic properties.
- In vitro testing of antibacterial, antifungal, anti-biofilm, hemolytic, and cytotoxicity effects.
Main Results:
- The designed peptide mCHTL131-140 demonstrated potent antibacterial activity against Acinetobacter baumannii.
- The peptide exhibited moderate antifungal properties.
- No significant hemolytic activity or cytotoxicity towards human fibroblast cells was observed.
Conclusions:
- The designed peptide mCHTL131-140 shows promise as a therapeutic agent against Acinetobacter baumannii.
- This novel AMP could be a valuable tool in controlling hospital-acquired infections.
- The peptide's safety profile suggests potential for further development.
