Spectroscopic studies on binding of 1-phenyl-3-(coumarin-6-yl)sulfonylurea to bovine serum albumin

Liu, Xiaohui; Xi, Pin-xian; Chen, Fengjuan; Xu, Zheng; Zeng, Zhengzhi

doi:10.1016/j.jphotobiol.2008.04.008

Cited by 61 publications

(17 citation statements)

References 18 publications

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“…8) This is true even of fatty acid binding which induces large rigid-body rotation of the protein domains. 6,19) Thus crystallographic investigation provides no corroboration of claims, usually based on CD measurement 80,81) that ligand binding results in substantial change in the secondary structure content of the protein.…”

Section: Fatty Acid Bindingmentioning

confidence: 98%

Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin

Curry

2009

Drug Metabolism and Pharmacokinetics

260

279

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Human serum albumin (HSA) is an abundant and highly soluble plasma protein with the capacity to bind a remarkably diverse set of lipophilic anionic compounds so that it fulfils important roles in the transport of nutrients, hormones and toxins. The protein attracts great interest from the pharmaceutical industry since it can also bind a variety of drug molecules, impacting their delivery and efficacy. Our understanding of the binding and transport properties of albumin has been transformed by structural studies of the protein, in which crystallographic analysis has played a leading role. This review summarises the main insights to have accrued from this work, highlighting the significant advances that have been made but also pointing out some of the challenges ahead. Since further progress is likely to benefit from increased structural scrutiny of HSA, methodological developments instrumental to the success of crystallographic analysis of the protein are discussed in some detail.

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Section: Fatty Acid Bindingmentioning

confidence: 98%

Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin

Curry

2009

Drug Metabolism and Pharmacokinetics

260

279

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“…When small molecules bind independently to equivalent sites on a macromolecule via a static fluorescence quenching mechanism, the relevant parameters including the number of binding sites ( n ) and the binding constant can be determined based on the following equation [29,30].

lg \frac{(F_{0} - F)}{F} = lg K_{normala} + n lg [Q]

where F 0 , F , and [ Q ] are the same as in Equation (1), K a is the binding constant and n is the number of binding sites.…”

Section: Resultsmentioning

confidence: 99%

Molecular Insights into the Potential Toxicological Interaction of 2-Mercaptothiazoline with the Antioxidant Enzyme—Catalase

Huang

et al. 2016

IJMS

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2-mercaptothiazoline (2-MT) is widely used in many industrial fields, but its residue is potentially harmful to the environment. In this study, to evaluate the biological toxicity of 2-MT at protein level, the interaction between 2-MT and the pivotal antioxidant enzyme—catalase (CAT) was investigated using multiple spectroscopic techniques and molecular modeling. The results indicated that the CAT fluorescence quenching caused by 2-MT should be dominated by a static quenching mechanism through formation of a 2-MT/CAT complex. Furthermore, the identifications of the binding constant, binding forces, and the number of binding sites demonstrated that 2-MT could spontaneously interact with CAT at one binding site mainly via Van der Waals’ forces and hydrogen bonding. Based on the molecular docking simulation and conformation dynamic characterization, it was found that 2-MT could bind into the junctional region of CAT subdomains and that the binding site was close to enzyme active sites, which induced secondary structural and micro-environmental changes in CAT. The experiments on 2-MT toxicity verified that 2-MT significantly inhibited CAT activity via its molecular interaction, where 2-MT concentration and exposure time both affected the inhibitory action. Therefore, the present investigation provides useful information for understanding the toxicological mechanism of 2-MT at the molecular level.

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“…For the static quenching interaction, when small molecules bind independently to a set of equivalent sites on a protein, the binding constant (K a ) and the number of binding sites (n) can be determined [35]. The relationship between the fluorescence intensity and the quenching medium can be deduced from the formula [36]:…”

Section: Binding Constant and Binding Capacitymentioning

confidence: 99%

The interaction between 4-aminoantipyrine and bovine serum albumin: Multiple spectroscopic and molecular docking investigations

Teng

Liu

et al. 2011

Journal of Hazardous Materials

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Spectroscopic studies on binding of 1-phenyl-3-(coumarin-6-yl)sulfonylurea to bovine serum albumin

Cited by 61 publications

References 18 publications

Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin

Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin

Molecular Insights into the Potential Toxicological Interaction of 2-Mercaptothiazoline with the Antioxidant Enzyme—Catalase

The interaction between 4-aminoantipyrine and bovine serum albumin: Multiple spectroscopic and molecular docking investigations

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