Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach

Lee, Wei Qi; Affandi, Ida Syazwani M; Feroz, Shevin Rizal; Mohamad, Saharuddin Bin; Tayyab, Saad

doi:10.1002/jbt.21839

Cited by 10 publications

(5 citation statements)

References 48 publications

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“…The value of the Stern–Volmer constant, K sv was determined from the slope of the Stern–Volmer plot. As can be seen from Table , the PM–GSA system had a value of K sv as 2.99 ± 0.03 × 10 5 M −1 , which was found to be similar to the K sv value (1.50 ± 0.01 × 10 5 M −1 ), reported for PM–human serum albumin system . The value of the bimolecular quenching rate constant, k q , as calculated from the K sv value, dropped into the range of 10 13 M −1 s −1 .…”

Section: Resultssupporting

confidence: 78%

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Exploring ligand–protein interaction: A laboratory exercise on herbicide binding to plasma transport protein

Roslan

Tayyab

2019

Biochem Molecular Bio Educ

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A laboratory exercise on the interaction between the herbicide pendimethalin (PM) and goat serum albumin (GSA), a carrier protein present in mammalian blood circulation, is described. Fluorescence spectroscopy was used to study the binding reaction between PM and GSA. Titration of a constant amount of the protein (GSA) with increasing ligand (PM) concentrations produced a consecutive decrease in the protein's fluorescence. Treatment of the fluorescence quenching data according to the Stern-Volmer equation yielded the values of the Stern-Volmer constant (K sv ) and bimolecular quenching rate constant (k q ), whereas values of the binding constant (K a ) and number of binding sites (n) were obtained from the double logarithmic plot. This experiment provides an exciting opportunity for undergraduate students to independently perform ligand binding studies with a protein, in addition to providing the means for the determination of their binding parameters.

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Section: Resultssupporting

confidence: 78%

“…Value of n (Table ) also suggested the presence of a single PM binding site in GSA. In a recent study, a similar binding affinity ( K a = 2.09 ± 0.06 × 10 5 m −1 ) was reported between PM and human serum albumin . Such a binding affinity suggested an efficient transportation of PM in goat blood circulation.…”

Section: Resultssupporting

confidence: 65%

Exploring ligand–protein interaction: A laboratory exercise on herbicide binding to plasma transport protein

Roslan

Tayyab

2019

Biochem Molecular Bio Educ

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“…Albumin is not just passive, but an active participant in pharmacokinetic and toxicokinetic processes too. The esterase or pseudoesterase activity of albumin against α-naphthyl acetate and p -nitrophenyl acetate (NPA), FA esters, aspirin, ketoprofen glucuronide, cyclophosphamide, nicotinic acid esters, octanoyl-ghrelin, nitroacetanilide, p -nitrofluoroacetanilide and some OPs have been demonstrated in numerous experiments [ 56 , 66 , 67 , 68 ]. A typical example of the pseudoesterase activity of albumin is acetylation.…”

Section: Enzymatic Activity Of Albuminmentioning

confidence: 99%

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Belinskaia

Voronina

Шмурак

et al. 2021

IJMS

163

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Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions—electrically neutral and charged molecules—and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind to almost all known drugs, as well as many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. Albumin of humans and respective representatives in cattle and rodents have their own structural features that determine species differences in functional properties. However, albumin is not only passive, but also an active participant of pharmacokinetic and toxicokinetic processes, possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogeneous and exogeneous esters. Due to the free thiol group of Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interactions with endothelial glycocalyx and vascular endothelial cells largely determine the integrative role of albumin. This review considers the esterase, antioxidant, transporting and signaling properties of albumin, as well as its structural and functional modifications and their significance in the pathogenesis of certain diseases.

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“…As shown in Figure S5, peak a and peak b corresponded to the Rayleigh scattering peak (λ em = λ ex ) and the second-order scattering peak (λ em = 2λ ex ), respectively. 54,55 Moreover, peak 1 (the strong fluorescence peak) primarily revealed the spectral behavior of Trp and Tyr residues. 56 From Table S3, it could be found that an obvious reduction in the fluorescence intensity of peak 1 (for α-amylase, decreased by 28.65%; for α-glucosidase, decreased by 32.43%) was observed, and a red shift in the peak position was recorded (for the α- amylase−silibinin system, 3 nm; for the α-glucosidase− silibinin system, 4 nm) when silibinin was added into the enzyme solution.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Yang

Wang

et al. 2021

J. Agric. Food Chem.

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As a natural flavonolignan, silibinin is reported to possess multiple biological activities, while the inhibitory potential of silibinin on carbohydrate-hydrolyzing enzymes is still unclear. Therefore, in this study, the inhibitory effect and underlying mechanism of silibinin against α-amylase/α-glucosidase were investigated. The results indicated that silibinin showed a strong inhibitory efficiency against α-amylase/α-glucosidase in noncompetitive manners and exhibited synergistic inhibition against αglucosidase with acarbose. However, interestingly, the inhibitory effect of silibinin was significantly hindered in various milk proteinrich environments, but this phenomenon disappeared after simulated gastrointestinal digestion of milk proteins in vitro. Furthermore, silibinin could combine with the inactive site of α-amylase/α-glucosidase and change the microenvironment and secondary structure of the enzymes, thereby influencing the catalytic efficiency of enzymes. This research suggested that silibinin could be used as a novel carbohydrate-hydrolyzing enzyme inhibitor, and milk beverages rich in silibinin had the potential for further application in antidiabetic dietary or medicine.

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Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach

Cited by 10 publications

References 48 publications

Exploring ligand–protein interaction: A laboratory exercise on herbicide binding to plasma transport protein

Exploring ligand–protein interaction: A laboratory exercise on herbicide binding to plasma transport protein

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

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