| Autor: |
Contreras F; Centro de Genómica y Bioinformática, Facultad de Ciencias, Universidad Mayor, Santiago, Chile., Rivas-Pardo JA; Centro de Genómica y Bioinformática, Facultad de Ciencias, Universidad Mayor, Santiago, Chile. jaime.rivas@umayor.cl. |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2020; Vol. 2136, pp. 347-364. |
| DOI: |
10.1007/978-1-0716-0467-0_28 |
| Abstrakt: |
Gram-positive bacteria use their adhesive pili to attach to host cells during early stages of a bacterial infection. These extracellular hair-like appendages experience mechanical stresses of hundreds of picoNewtons; however, the presence of an internal isopeptide bond prevents the pilus protein from unfolding. Here, we describe a method to interfere with nascent pili proteins through a peptide that mimics one of the β-strands of the molecule. By using AFM-based force spectroscopy, we study the isopeptide bond formation and the effect of the peptide in the elasticity of the pilus protein. This method could be used to afford a new strategy for mechanically targeted antibiotics by simply blocking the folding of the bacterial pilus protein. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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