Interaction of chloramphenicol with titin I27 probed using single-molecule force spectroscopy.

ABSTRACT: Titin is a giant elastic protein which is responsible for passive muscle stiffness when muscle sarcomeres are stretched. Chloramphenicol, besides being a broad-spectrum antibiotic, also acts as a muscle relaxant. Therefore, it is important to study the interaction between titin I27 and chloramphenicol. We investigated the interaction of chloramphenicol with octamer of titin I27 using single-molecule force spectroscopy and fluorescence spectroscopy. The fluorescence data indicated that binding of chloramphenicol with I27 results in fluorescence quenching. Furthermore, it is observed that chloramphenicol binds to I27 at a particular concentration ([Formula: see text] 40 μM). Single-molecule force spectroscopy shows that, in the presence of 40 μM chloramphenicol concentration, the I27 monomer

SUBMITTER: Yadav J 

PROVIDER: S-EPMC8184918 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature