Development of Bactericidal Peptides against Multidrug-Resistant Acinetobacter baumannii with Enhanced Stability and Low Toxicity
Pathogenic superbugs are the root cause of untreatable complex infections with limited or no treatment options. These infections are becoming more common as clinical antibiotics have lost their effectiveness over time. Therefore, the development of novel antibacterial agents is urgently needed to co...
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Veröffentlicht in: | International journal of molecular sciences 2022-02, Vol.23 (4), p.2191 |
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creator | Hazam, Prakash Kishore Cheng, Chin-Cheng Hsieh, Chu-Yi Lin, Wen-Chun Hsu, Po-Hsien Chen, Te-Li Lee, Yi-Tzu Chen, Jyh-Yih |
description | Pathogenic superbugs are the root cause of untreatable complex infections with limited or no treatment options. These infections are becoming more common as clinical antibiotics have lost their effectiveness over time. Therefore, the development of novel antibacterial agents is urgently needed to counter these microbes. Antimicrobial peptides (AMPs) are a viable treatment option due to their bactericidal potency against multiple microbial classes. AMPs are naturally selected physiological microbicidal agents that are found in all forms of organisms. In the present study, we developed two tilapia piscidin 2 (TP2)-based AMPs for antimicrobial application. Unlike the parent peptide, the redesigned peptides showed significant antimicrobial activity against multidrug-resistant bacterial species. These peptides also showed minimal cytotoxicity. In addition, they were significantly active in the presence of physiological salts, 50% human serum and elevated temperature. The designed peptides also showed synergistic activity when combined with clinical antibiotics. The current approach demonstrates a fruitful strategy for developing potential AMPs for antimicrobial application. Such AMPs have potential for progression to further trials and drug development investigations. |
doi_str_mv | 10.3390/ijms23042191 |
format | Article |
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These infections are becoming more common as clinical antibiotics have lost their effectiveness over time. Therefore, the development of novel antibacterial agents is urgently needed to counter these microbes. Antimicrobial peptides (AMPs) are a viable treatment option due to their bactericidal potency against multiple microbial classes. AMPs are naturally selected physiological microbicidal agents that are found in all forms of organisms. In the present study, we developed two tilapia piscidin 2 (TP2)-based AMPs for antimicrobial application. Unlike the parent peptide, the redesigned peptides showed significant antimicrobial activity against multidrug-resistant bacterial species. These peptides also showed minimal cytotoxicity. In addition, they were significantly active in the presence of physiological salts, 50% human serum and elevated temperature. The designed peptides also showed synergistic activity when combined with clinical antibiotics. The current approach demonstrates a fruitful strategy for developing potential AMPs for antimicrobial application. Such AMPs have potential for progression to further trials and drug development investigations.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms23042191</identifier><identifier>PMID: 35216307</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Acinetobacter baumannii ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Anti-Infective Agents - pharmacology ; Antibacterial agents ; Antibiotics ; Antiinfectives and antibacterials ; Antimicrobial activity ; Antimicrobial agents ; Antimicrobial peptides ; Clinical trials ; Cytotoxicity ; Drug development ; Drug resistance ; Drug Resistance, Multiple, Bacterial ; Heat resistance ; High temperature ; Humans ; Microbial Sensitivity Tests ; Microbicides ; Microorganisms ; Multidrug resistance ; Multidrug resistant organisms ; Peptides ; Physiology ; Salts ; Surfactants ; Tilapia ; Toxicity</subject><ispartof>International journal of molecular sciences, 2022-02, Vol.23 (4), p.2191</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). 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These infections are becoming more common as clinical antibiotics have lost their effectiveness over time. Therefore, the development of novel antibacterial agents is urgently needed to counter these microbes. Antimicrobial peptides (AMPs) are a viable treatment option due to their bactericidal potency against multiple microbial classes. AMPs are naturally selected physiological microbicidal agents that are found in all forms of organisms. In the present study, we developed two tilapia piscidin 2 (TP2)-based AMPs for antimicrobial application. Unlike the parent peptide, the redesigned peptides showed significant antimicrobial activity against multidrug-resistant bacterial species. These peptides also showed minimal cytotoxicity. In addition, they were significantly active in the presence of physiological salts, 50% human serum and elevated temperature. The designed peptides also showed synergistic activity when combined with clinical antibiotics. The current approach demonstrates a fruitful strategy for developing potential AMPs for antimicrobial application. 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These infections are becoming more common as clinical antibiotics have lost their effectiveness over time. Therefore, the development of novel antibacterial agents is urgently needed to counter these microbes. Antimicrobial peptides (AMPs) are a viable treatment option due to their bactericidal potency against multiple microbial classes. AMPs are naturally selected physiological microbicidal agents that are found in all forms of organisms. In the present study, we developed two tilapia piscidin 2 (TP2)-based AMPs for antimicrobial application. Unlike the parent peptide, the redesigned peptides showed significant antimicrobial activity against multidrug-resistant bacterial species. These peptides also showed minimal cytotoxicity. In addition, they were significantly active in the presence of physiological salts, 50% human serum and elevated temperature. The designed peptides also showed synergistic activity when combined with clinical antibiotics. 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subjects | Acinetobacter baumannii Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Anti-Infective Agents - pharmacology Antibacterial agents Antibiotics Antiinfectives and antibacterials Antimicrobial activity Antimicrobial agents Antimicrobial peptides Clinical trials Cytotoxicity Drug development Drug resistance Drug Resistance, Multiple, Bacterial Heat resistance High temperature Humans Microbial Sensitivity Tests Microbicides Microorganisms Multidrug resistance Multidrug resistant organisms Peptides Physiology Salts Surfactants Tilapia Toxicity |
title | Development of Bactericidal Peptides against Multidrug-Resistant Acinetobacter baumannii with Enhanced Stability and Low Toxicity |
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