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Updated: Dec 31, 2025

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Host Defense Peptide Mimicking Peptide Polymer Exerting Fast, Broad Spectrum, and Potent Activities toward Clinically
Sheng Chen1,2, Xiaoyan Shao2, Ximian Xiao1
1State Key Laboratory of Bioreactor Engineering, Key Laboratory for Ultrafine Materials of Ministry of Education, Research Center for Biomedical Materials of Ministry of Education, Key Laboratory of Specially Functional Polymeric Materials and Related Technology (ECUST), Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai 200237, China.
Abstract:
Multidrug-resistant (MDR) bacteria have emerged quickly and have caused serious nosocomial infections. It is urgent to develop novel antimicrobial agents for treating MDR bacterial infections. In this study, we isolated 45 strains of bacteria from hospital patients and found shockingly that most of these strains were MDR to antimicrobial drugs. This inspired us to explore antimicrobial peptide polymers as synthetic mimics of host defense peptides in combating drug-resistant bacteria and the formidable antimicrobial challenge. We found that peptide polymer 80:20 DM:Bu (where DM is a hydrophilic/cationic subunit and Bu is a hydrophobic subunit) displayed fast bacterial killing, broad spectrum, and potent activity against clinically isolated strains of MDR bacteria. Moreover, peptide polymer 80:20 DM:Bu displayed potent in vivo antibacterial efficacy, comparable to the performance of polymyxin B, in a Pseudomonas aeruginosa (P. aeruginosa) infected rat full-thickness wound model. The peptide polymer can be easily synthesized from ring-opening polymerization with remarkable reproducibility in structural properties and biological activities. The peptide polymer's potent and broad spectrum antimicrobial activities against MDR bacteria in vitro and in vivo, resistance to proteolysis, and high structural diversity altogether imply a great potential of peptide polymer 80:20 DM:Bu in antimicrobial applications as synthetic mimics of host defense peptides.
Insights
Novel peptide polymers show potent activity against multidrug-resistant (MDR) bacteria. This synthetic mimic of host defense peptides offers a promising solution for treating serious nosocomial infections caused by drug-resistant bacteria.
Area of Science:
- Biochemistry
- Polymer Chemistry
- Microbiology
Background:
- Multidrug-resistant (MDR) bacteria pose a significant threat, causing severe nosocomial infections.
- There is an urgent need for novel antimicrobial agents to combat drug-resistant bacterial infections.
- Host defense peptides (HDPs) offer a natural model for antimicrobial strategies.
Purpose of the Study:
- To explore antimicrobial peptide polymers as synthetic mimics of HDPs.
- To evaluate the efficacy of peptide polymer 80:20 DM:Bu against clinically isolated MDR bacteria.
- To assess the in vivo antibacterial performance of the peptide polymer.
Main Methods:
- Isolation and characterization of 45 bacterial strains from hospital patients.
- Synthesis of peptide polymer 80:20 DM:Bu via ring-opening polymerization.
- In vitro antimicrobial activity testing and in vivo efficacy evaluation in a rat wound model infected with Pseudomonas aeruginosa.
Main Results:
- Most isolated bacterial strains exhibited multidrug resistance.
- Peptide polymer 80:20 DM:Bu demonstrated fast bacterial killing, broad-spectrum activity, and potent efficacy against MDR bacteria in vitro.
- The peptide polymer showed comparable in vivo antibacterial efficacy to polymyxin B in a P. aeruginosa wound model.
Conclusions:
- Peptide polymer 80:20 DM:Bu is a promising synthetic mimic of HDPs for combating MDR bacteria.
- The peptide polymer exhibits potent in vitro and in vivo antimicrobial activities, resistance to proteolysis, and structural diversity.
- Easy synthesis and reproducibility suggest significant potential for peptide polymer 80:20 DM:Bu in antimicrobial applications.
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