The hydrophobic cluster on the surface of protein is the key structural basis for the SDS-resistance of chondroitinase VhChlABC.

ABSTRACT: The application of chondroitinase requires consideration of the complex microenvironment of the target. Our previous research reported a marine-derived sodium dodecyl sulfate (SDS)-resistant chondroitinase VhChlABC. This study further investigated the mechanism of VhChlABC resistance to SDS. Focusing on the hydrophobic cluster on its strong hydrophilic surface, it was found that the reduction of hydrophobicity of surface residues Ala¹⁸¹, Met¹⁸², Met¹⁸³, Ala¹⁸⁴, Val¹⁸⁵, and Ile³⁰⁵ significantly reduced the SDS resistance and stability. Molecular dynamics (MD) simulation and molecular docking analysis showed that I305G had more conformational flexibility around residue 305 than wild type (WT), which was more conducive to SDS i

SUBMITTER: Su J 

PROVIDER: S-EPMC10902247 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature