Affiliation:
1. Department of Biology and Chemistry Paul Scherrer Institute Villigen 5232 Switzerland
2. Science Division New York University Abu Dhabi Saadiyat Island Abu Dhabi 129188 UAE
3. Department of Biochemistry and Biophysics Stockholm University Stockholm 106 91 Sweden
4. Department of Pathology and Microbiology, University of Nebraska Medical Center 985900 Nebraska Medical Center Omaha NE 68198‐5900 USA
Abstract
AbstractOligomerization of antimicrobial peptides (AMPs) is critical in their effects on pathogens. LL‐37 and its truncated fragments are widely investigated regarding their structures, antimicrobial activities, and application, such as developing new antibiotics. Due to the small size and weak intermolecular interactions of LL‐37 fragments, it is still elusive to establish the relationship between oligomeric states and antimicrobial activities. Here, an α‐hemolysin nanopore, mass spectrometry (MS), and molecular dynamic (MD) simulations are used to characterize the oligomeric states of two LL‐37 fragments. Nanopore studies provide evidence of trapping events related to the oligomer formation and provide further details on their stabilities, which are confirmed by MS and MD simulations. Furthermore, simulation results reveal the molecular basis of oligomer dynamics and states of LL‐37 fragments. This work provides unique insights into the relationship between the oligomer dynamics of AMPs and their antimicrobial activities at the single‐molecule level. The study demonstrates how integrating methods allows deciphering single molecule level understanding from nanopore sensing approaches.
Funder
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
China Scholarship Council
Subject
Biomaterials,Biotechnology,General Materials Science,General Chemistry
Cited by
5 articles.
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