Flipping out: role of arginine in hydrophobic interactions and biological formulation design.

ABSTRACT: Arginine has been a mainstay in biological formulation development for decades. To date, the way arginine modulates protein stability has been widely studied and debated. Here, we employed a hydrophobic polymer to decouple hydrophobic effects from other interactions relevant to protein folding. While existing hypotheses for the effects of arginine can generally be categorized as either direct or indirect, our results indicate that direct and indirect mechanisms of arginine co-exist and oppose each other. At low concentrations, arginine was observed to stabilize hydrophobic polymer folding via a sidechain-dominated direct mechanism, while at high concentrations, arginine stabilized polymer folding via a backbone-dominated indirect mechanism. Upon introducing partially charged

SUBMITTER: Zajac JWP 

PROVIDER: S-EPMC11915020 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature