Interaction of Anionic Surfactants with Native and Partially Unfolded RNase A: Binding Kinetics, Structural Changes, and Stability.

ABSTRACT: In protein-surfactant interactions, the alkyl chain length of surfactants and the surface-exposed residues of proteins play essential roles in binding and unfolding. To investigate this, the interactions of sodium octyl (SOS), decyl (SDeS), and dodecyl (SDoS) sulfates were studied with native and partially unfolded forms of ribonuclease A (ox-RNase A and rd-RNase A) by using surface plasmon resonance (SPR), optical spectroscopy, and molecular dynamics (MD) simulations. rd-RNase A was obtained by partial reduction of the disulfide bonds of RNase A. MD simulations of RNase A in its native and unfolded states were carried out in the presence of all three surfactants in their monomeric and micellar concentrations, respectively. The binding affinity of surfactants differs between ox-RNase A and

SUBMITTER: Kumar S 

PROVIDER: S-EPMC12223854 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature