A molecular simulation approach towards the development of universal nanocarriers by studying the pH- and electrostatic-driven changes in the dynamic structure of albumin.

ABSTRACT: To explore the intramolecular interactions of protein, and its folding and unfolding mechanisms, we performed a simulation-based comparative study on albumin at different ionic strengths and pH. In this study, we performed molecular dynamics (MD) simulation for bovine serum albumin (BSA) at five different concentrations of NaCl (10, 20, 30, 40 and 50 mM), and five different pH values (2.0, 3.5, 4.3, 7.4, and 9.0). Herein, our aim was to unravel the effects of both pH and ionic strength on the conformations of the serum albumin structure. Our results indicate the effects of physicochemical factors in promoting conformational changes in the albumin structure, unlocking the hydrophobic sequences for hydrophobic drug binding. The BSA structure showed similarity to its native state in the pH ra

SUBMITTER: Srivastav AK 

PROVIDER: S-EPMC9051469 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature