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  3. Self-Assembling and Pore-Forming Peptoids as Antimicrobial Biomaterials

Self-Assembling and Pore-Forming Peptoids as Antimicrobial Biomaterials

  • ACS Nano. 2024 Aug 27;18(34):23077-23089. doi: 10.1021/acsnano.4c05250.
Tengyue Jian 1,  Minghui Wang 2,  Jeevapani Hettige 1,  Yuhao Li 3,  Lei Wang 1 4,  Ruixuan Gao 2,  Wenchao Yang 1,  Renyu Zheng 1 5,  Shengliang Zhong 4,  Marcel D Baer 1,  Aleksandr Noy 3 6,  James J De Yoreo 1 7,  Jianfeng Cai 2,  Chun-Long Chen 1 5
Affiliations

Affiliations

  • 1 Physical Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.
  • 2 Department of Chemistry, University of South Florida, Tampa, Florida 33620, United States.
  • 3 Materials Science Division, Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, California 94550, United States.
  • 4 College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, Jiangxi, China.
  • 5 Department of Chemical Engineering, University of Washington, Seattle, Washington 98195, United States.
  • 6 School of Natural Sciences, University of California, Merced, Merced, California 95343, United States.
  • 7 Department of Materials Science and Engineering, University of Washington, Seattle, Washington 98195, United States.
PMID: 39146502 DOI: 10.1021/acsnano.4c05250
Abstract

Bacterial infections have been a serious threat to mankind throughout history. Natural antimicrobial peptides (AMPs) and their membrane disruption mechanism have generated immense interest in the design and development of synthetic mimetics that could overcome the intrinsic drawbacks of AMPs, such as their susceptibility to proteolytic degradation and low bioavailability. Herein, by exploiting the self-assembly and pore-forming capabilities of sequence-defined peptoids, we discovered a family of low-molecular weight peptoid Antibiotics that exhibit excellent broad-spectrum activity and high selectivity toward a panel of clinically significant Gram-positive and Gram-negative Bacterial strains, including vancomycin-resistant Enterococcus faecalis (VREF), methicillin-resistant Staphylococcus aureus (MRSA), methicillin-resistant Staphylococcus epidermidis (MRSE), Escherichia coli, Pseudomonas aeruginosa, and Klebsiella pneumoniae. Tuning the peptoid side chain chemistry and structure enabled us to tune the efficacy of antimicrobial activity. Mechanistic studies using transmission electron microscopy (TEM), Bacterial membrane depolarization and lysis, and time-kill kinetics assays along with molecular dynamics simulations reveal that these peptoids kill both Gram-positive and Gram-negative bacteria through a membrane disruption mechanism. These robust and biocompatible peptoid-based Antibiotics can provide a valuable tool for combating emerging drug resistance.

Keywords

antimicrobial activity; membrane disruption; peptoid; pore formation; self-assembly.

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