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

Cited by 2 publications

(3 citation statements)

References 53 publications

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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%

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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“…Serum albumins play many significant roles in the body for normal physiological functioning, like transporting hormones, drugs, bile acid, and amino acids to the specific target subdomain and maintaining oncotic pressure. [4,5] Besides these, serum albumins are also involved in many vital biological processes like anticoagulation, inhibition of platelet aggregation, and removal of radicals. The reference range of SAs in blood plasma is 30-50 g L À 1 , while 5-25 mg L À 1 in urine.…”

Section: Introductionmentioning

confidence: 99%

“…3 Serum albumins (SAs) are exclusively synthesized by the liver, with an average life of 19–21 days in the blood vascular system, and then eliminated by the kidney. Serum albumins play many significant roles in the body for normal physiological functioning, like transporting hormones, drugs, bile acid, and amino acids to the specific target subdomain and maintaining oncotic pressure [4,5] . Besides these, serum albumins are also involved in many vital biological processes like anticoagulation, inhibition of platelet aggregation, and removal of radicals.…”

Section: Introductionmentioning

confidence: 99%

Investigating the Serum Albumin Binding Behavior of Naphthalimide Based Fluorophore Conjugates: Spectroscopic and Molecular Docking Approach

Gupta,

Paul

2024

ChemMedChem

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In the present study, naphthalimide‐pyrazole‐benzothiazole based fluorescent analogs were synthesized by substituting different primary and secondary amines on the naphthalimide nucleus and were evaluated for their sensitivity and selectivity towards serum albumin. Among various synthesized analogues compound 25 showed the most significant change with serum albumin and was further studied for selective detection and mode of interaction with serum albumin. Here, we compared the binding interaction of fluorescent probe 25 for variation/detection of two 76% structurally resembling proteins HSA and BSA, by spectroscopic experiments. The compound shows more selectivity for HSA and BSA with a higher binding constant and evident visible change in the emission spectra of two serum albumins among different bioanalytes. The mode of interaction of 25 with human serum albumin and bovine serum albumin was investigated by FT‐IR, circular dichroism, and DLS techniques to find out the change in the microenvironment and variation in the structure of serum albumin proteins. Higher binding affinity and specific selectivity of 25 with a limit of detection of 0.69 µM and 1.4 µM towards HSA and BSA compared to other bioanalytes make it a significant fluorescent probe for quantitatively detecting serum albumins at the very early stage of many fatal diseases.

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

Cited by 2 publications

References 53 publications

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

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

Investigating the Serum Albumin Binding Behavior of Naphthalimide Based Fluorophore Conjugates: Spectroscopic and Molecular Docking Approach

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