Photophysical properties and dynamics simulation of the interaction between human serum albumin and hydroxy polybrominated diphenyl ether

Wei, Yuchen; Xu, Jide; Huang, Muwei; Rui, Yuefan; Wu, Zhiwei Steven; Yi, Zhongsheng

doi:10.1080/00387010.2022.2029492

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2022

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“…The increase in compound hydrophobicity likely contributes to more effective binding within the HSA hydrophobic domains. The introduction of amino (entry 4) or hydroxyl 34 (entry 5) decreases binding affinity, although the polar surface area would be increased. These groups on the diphenyl ether scaffold reduce the binding affinity by nearly 9-and 2-fold, suggesting a binding penalty for a hydrophobic domain within HSA to accommodate the polar groups.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Using Human Serum Albumin Binding Affinities as a Proactive Strategy to Affect the Pharmacodynamics and Pharmacokinetics of Preclinical Drug Candidates

Fan

Gilmartin

Octaviano

et al. 2022

ACS Pharmacol. Transl. Sci.

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We report on a new preclinical drug optimization strategy that measures drug candidates’ binding affinity with human serum albumin (HSA) as an assessment of increasing or decreasing serum T1/2. Three common scaffolds were used as drug prototypes. Common polar and nonpolar substituents attached to the scaffolds have been identified as opportunities for increasing or decreasing the HSA binding affinity. This approach of adjusting HSA binding could be proactively established for preclinical drug candidates by appending functionality to sites on the drug scaffold not involved in biological target interactions. This strategy complements other medicinal chemistry efforts to identify longer or shorter human dosing regimens.

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Section: ■ Results and Discussionmentioning

confidence: 99%