Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves
Aims: Antibiotic resistance is currently a major challenge to scientists. Thus, attempts have been made to develop new compounds with antimicrobial activity. In this research, a new antimicrobial peptide with antibacterial activity was isolated from the plant Urtica dioica . Methods: A new antimicro...
Saved in:
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
SAGE Publishing
2025-01-01
|
Series: | Bioinformatics and Biology Insights |
Online Access: | https://doi.org/10.1177/11779322251315291 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
_version_ | 1832582435917791232 |
---|---|
author | Mahnaz Nasre Taheri Sima Sadat Seyedjavadi Mehdi Goudarzi Gholamhossein Ebrahimipour Ali Hashemi |
author_facet | Mahnaz Nasre Taheri Sima Sadat Seyedjavadi Mehdi Goudarzi Gholamhossein Ebrahimipour Ali Hashemi |
author_sort | Mahnaz Nasre Taheri |
collection | DOAJ |
description | Aims: Antibiotic resistance is currently a major challenge to scientists. Thus, attempts have been made to develop new compounds with antimicrobial activity. In this research, a new antimicrobial peptide with antibacterial activity was isolated from the plant Urtica dioica . Methods: A new antimicrobial peptide, named cliotide U1, was purified through precipitation with ammonium sulfate and reverse-phase high-performance liquid chromatography. In silico methods analyzed the physicochemical properties of cliotide U1. The properties of the peptide, including antibacterial activity, pH stability, heat stability, cytotoxicity, and hemolytic activity, were also examined. Findings: The purified peptide was composed of 35 amino acids with a hydrophobicity ratio of 63% and a net charge of + 5. The antibacterial activity of cliotide U1 was observed against gram-negative and gram-positive bacteria with a minimum inhibitory concentration (MIC) of 1 to 4 µM. Cliotide U1 had less than 2% cytotoxic activity at the MIC range against the human embryonic kidney cell line 293 with no clear hemolytic activity. The stability of cliotide U1 was preserved at various temperatures (10-60°C) and pH (6-9). Conclusion: Our results demonstrated that cliotide U1 had potent antibacterial potential against gram-negative and gram-positive bacteria. Considering its properties, cliotide U1 can be introduced as a novel antibacterial candidate for expanding new therapeutic drugs. |
format | Article |
id | doaj-art-359ea7edf8b44e17ba343a661663f2f1 |
institution | Kabale University |
issn | 1177-9322 |
language | English |
publishDate | 2025-01-01 |
publisher | SAGE Publishing |
record_format | Article |
series | Bioinformatics and Biology Insights |
spelling | doaj-art-359ea7edf8b44e17ba343a661663f2f12025-01-29T17:03:41ZengSAGE PublishingBioinformatics and Biology Insights1177-93222025-01-011910.1177/11779322251315291Cliotide U1, a Novel Antimicrobial Peptide Isolated From LeavesMahnaz Nasre Taheri0Sima Sadat Seyedjavadi1Mehdi Goudarzi2Gholamhossein Ebrahimipour3Ali Hashemi4Department of Microbiology, Faculty of Biological Sciences and Technology, Shahid Beheshti University, Tehran, IranDepartment of Mycology, Pasteur Institute of Iran, Tehran, IranInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, IranDepartment of Microbiology, Faculty of Biological Sciences and Technology, Shahid Beheshti University, Tehran, IranDepartment of Microbiology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, IranAims: Antibiotic resistance is currently a major challenge to scientists. Thus, attempts have been made to develop new compounds with antimicrobial activity. In this research, a new antimicrobial peptide with antibacterial activity was isolated from the plant Urtica dioica . Methods: A new antimicrobial peptide, named cliotide U1, was purified through precipitation with ammonium sulfate and reverse-phase high-performance liquid chromatography. In silico methods analyzed the physicochemical properties of cliotide U1. The properties of the peptide, including antibacterial activity, pH stability, heat stability, cytotoxicity, and hemolytic activity, were also examined. Findings: The purified peptide was composed of 35 amino acids with a hydrophobicity ratio of 63% and a net charge of + 5. The antibacterial activity of cliotide U1 was observed against gram-negative and gram-positive bacteria with a minimum inhibitory concentration (MIC) of 1 to 4 µM. Cliotide U1 had less than 2% cytotoxic activity at the MIC range against the human embryonic kidney cell line 293 with no clear hemolytic activity. The stability of cliotide U1 was preserved at various temperatures (10-60°C) and pH (6-9). Conclusion: Our results demonstrated that cliotide U1 had potent antibacterial potential against gram-negative and gram-positive bacteria. Considering its properties, cliotide U1 can be introduced as a novel antibacterial candidate for expanding new therapeutic drugs.https://doi.org/10.1177/11779322251315291 |
spellingShingle | Mahnaz Nasre Taheri Sima Sadat Seyedjavadi Mehdi Goudarzi Gholamhossein Ebrahimipour Ali Hashemi Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves Bioinformatics and Biology Insights |
title | Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves |
title_full | Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves |
title_fullStr | Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves |
title_full_unstemmed | Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves |
title_short | Cliotide U1, a Novel Antimicrobial Peptide Isolated From Leaves |
title_sort | cliotide u1 a novel antimicrobial peptide isolated from leaves |
url | https://doi.org/10.1177/11779322251315291 |
work_keys_str_mv | AT mahnaznasretaheri cliotideu1anovelantimicrobialpeptideisolatedfromleaves AT simasadatseyedjavadi cliotideu1anovelantimicrobialpeptideisolatedfromleaves AT mehdigoudarzi cliotideu1anovelantimicrobialpeptideisolatedfromleaves AT gholamhosseinebrahimipour cliotideu1anovelantimicrobialpeptideisolatedfromleaves AT alihashemi cliotideu1anovelantimicrobialpeptideisolatedfromleaves |