Structural Insights into the Osteopontin-Aptamer Complex by Molecular Dynamics Simulations.

ABSTRACT: Osteopontin is an intrinsically disordered protein involved in tissue remodeling. As a biomarker for pathological hypertrophy and fibrosis, the protein is targeted by an RNA aptamer. In this work, we model the interactions between osteopontin and its aptamer, including mono- (Na⁺) and divalent (Mg²⁺) cations. The molecular dynamics simulations suggest that the presence of divalent cations forces the N-terminus of osteopontin to bind the shell of divalent cations adsorbed over the surface of its RNA aptamer, the latter exposing a high negative charge density. The osteopontin plasticity as a function of the local concentration of Mg is discussed in the frame of the proposed strategies for osteopontin targeting as biomarker and in theranostic.

SUBMITTER: La Penna G 

PROVIDER: S-EPMC5797602 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature