期刊
SCIENCE
卷 359, 期 6383, 页码 1527-1532出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar2094
关键词
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资金
- European Research Council (ERC) [294438]
- Deutsche Forschungsgemeinschaft (DFG) [Sonderforschungsbereich 1032]
- National Institutes of Health (NIH) Center for Macromolecular Modeling and Bioinformatics [P41-GM104601]
- National Science Foundation (NSF) [MCB-1616590]
- National Science Foundation [ACI-1440026, ACI-1713784, OCI-0725070, ACI-1238993]
- state of Illinois
High resilience to mechanical stress is key when pathogens adhere to their target and initiate infection. Using atomic force microscopy-based single-molecule force spectroscopy, we explored the mechanical stability of the prototypical staphylococcal adhesin SdrG, which targets a short peptide from human fibrinogen b. Steered molecular dynamics simulations revealed, and single-molecule force spectroscopy experiments confirmed, the mechanism by which this complex withstands forces of over 2 nanonewtons, a regime previously associated with the strength of a covalent bond. The target peptide, confined in a screwlike manner in the binding pocket of SdrG, distributes forces mainly toward the peptide backbone through an intricate hydrogen bond network. Thus, these adhesins can attach to their target with exceptionally resilient mechanostability, virtually independent of peptide side chains.
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