Eun Ju Lee

TL;DR: Based on encouraging data about the antibacterial effects of NP/antibiotic combinations, it is proposed that this concept be thoroughly researched to identify means of combating drug-resistant bacteria.

TL;DR: Thermodynamic analysis shows HSA-EH complex formation occurs primarily due to hydrophobic interactions, and hydrogen bonds were facilitated at the binding of EH, helping to understand the activity and mechanism of drug binding.

TL;DR: This extensive study provides additional insight of ligand binding and structural changes induced in HSA relevant to the biological activity of HSA in vivo.

TL;DR: In vitro interaction studies of EA with the primary plasma protein, human serum albumin, reveal a static mode of quenching with binding constant Kb ∼104 reflecting high affinity of EA for HSA and thermodynamic signatures of the HSA-EA interaction in the complex reflect dominance of hydrogen bonds.

TL;DR: It is indicated that the targeting of metabolic signaling offers a promising means of developing novel anti-cancer therapies.