Journal Article Research Support, Non-U.S. Gov't Ppublish 15 citations
PubMed: 37341246 DOI: 10.1002/advs.202302483
Real-Time Monitoring of Multitarget Antimicrobial Mechanisms of Peptoids Using Label-Free Imaging with Optical Diffraction Tomography.
Adv Sci (Weinh) 10(24):e2302483
Authors: Minsang Kim, Yeongmi Cheon, Dongmin Shin, Jieun Choi, Josefine Eilsø Nielsen, Myeong Seon Jeong, Ho Yeon Nam, Sung-Hak Kim, Reidar Lund, Håvard Jenssen, Annelise E Barron, Seongsoo Lee, Jiwon Seo
Affiliations
- Department of Chemistry, Gwangju Institute of Science and Technology (GIST), 123, Cheomdangwagi-ro, Buk-gu, Gwangju, 61005, Republic of Korea.
- Gwangju Center, Korea Basic Science Institute (KBSI), 49, Dosicheomdansaneop-ro, Nam-gu, Gwangju, 61751, Republic of Korea. Laboratory of Molecular Biochemistry, Chonnam National University, 77, Yongbong-ro, Buk-gu, Gwangju, 61186, Republic of Korea. Department of Microbiology and Molecular Biology, Chungnam National University, 99, Daehak-ro, Yuseong-gu, Daejeon, 34134, Republic of Korea.
- Department of Science and Environment, Roskilde University, Universitetsvej 1, Roskilde, 4000, Denmark.
- Department of Bioengineering, Schools of Medicine and Engineering, Stanford University, 443 Via Ortega, Stanford, California, 94305, United States.
- Chuncheon Center, Korea Basic Science Institute (KBSI), 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Republic of Korea.
- Laboratory of Molecular Biochemistry, Chonnam National University, 77, Yongbong-ro, Buk-gu, Gwangju, 61186, Republic of Korea.
- Department of Chemistry, University of Oslo, Problemveien 7, Oslo, 0315, Norway.
- Gwangju Center, Korea Basic Science Institute (KBSI), 49, Dosicheomdansaneop-ro, Nam-gu, Gwangju, 61751, Republic of Korea. Department of Systems Biotechnology, Chung-Ang University, Anseong-si, Gyeonggi-do, 17546, Republic of Korea.
Abstract
Antimicrobial peptides (AMPs) are promising therapeutics in the fight against multidrug-resistant bacteria. As a mimic of AMPs, peptoids with N-substituted glycine backbone have been utilized for antimicrobials with resistance against proteolytic degradation. Antimicrobial peptoids are known to kill bacteria by membrane disruption; however, the nonspecific aggregation of intracellular contents is also suggested as an important bactericidal mechanism. Here,structure-activity relationship (SAR) of a library of indole side chain-containing peptoids resulting in peptoid 29 as a hit compound is investigated. Then, quantitative morphological analyses of live bacteria treated with AMPs and peptoid 29 in a label-free manner using optical diffraction tomography (ODT) are performed. It is unambiguously demonstrated that both membrane disruption and intracellular biomass flocculation are primary mechanisms of bacterial killing by monitoring real-time morphological changes of bacteria. These multitarget mechanisms and rapid action can be a merit for the discovery of a resistance-breaking novel antibiotic drug.
MeSH
Bacteria, Membranes, N-Substituted Glycines, Biomedical Research, Tomography, Peptoids, Structure-Activity Relationship
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- Real-Time Monitoring of Multitarget Antimicrobial Mechanisms of Peptoids Using Label-Free Imaging with Optical Diffraction Tomography. Adv Sci (Weinh), 2023