Multiple Dynamically-Coupled Binding Sites on Human Serum Albumin Regulate Estradiol's Nonlinear Binding.

Mohammad Anees; Mark K. Fugate; Shalender Bhasin; Deeptanshu Pandey; Sourav Chowdhury; Ravi Jasuja

doi:10.1210/endocr/bqag027

March 12, 2026

Multiple Dynamically-Coupled Binding Sites on Human Serum Albumin Regulate Estradiol's Nonlinear Binding.

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Key Points

The study aims to understand how estradiol interacts with human serum albumin (HSA) beyond the traditional binding model.
Examined estradiol's interaction with human serum albumin.
Analyzed binding data beyond 1:1 stoichiometry and fixed Kd models.
Investigated ligand-induced conformational changes in HSA.
Found that estradiol binding to HSA is a dynamic process.
Demonstrated that multiple binding sites exist on HSA.
Indicated that traditional models do not fully explain the interactions.

Implication

Observations reveal estradiol's nonlinear binding to human serum albumin, suggesting complex multi-equilibrium interactions.

Abstract

Estradiol's binding to HSA is a dynamic, multi-equilibrium process driven by ligand-induced conformational rearrangements within HSA; the binding data are inconsistent with canonical model of estradiol-HSA interaction with 1:1 stoichiometry and a fixed Kd.

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Cite This Study

Anees et al. (2026) studied this question.

synapsesocial.com/papers/69b4b9eb18185d8a398021c3 https://doi.org/10.1210/endocr/bqag027

View Full Paper

Ask AI

Bookmark

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Multiple Dynamically-Coupled Binding Sites on Human Serum Albumin Regulate Estradiol's Nonlinear Binding.

Key Points

Implication

Abstract

Discussion

Cite This Study

Multiple Dynamically-Coupled Binding Sites on Human Serum Albumin Regulate Estradiol's Nonlinear Binding.

Key Points

Implication

Abstract

Discussion

Cite This Study

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