2021
DOI: 10.1038/s41598-021-83534-0
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Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches

Abstract: Monoisoamyl 2,3-dimercaptosuccinic acid (MiADMSA), a lipophilic chelator has been evaluated for its potential use as an antidote in arsenic poisoning. The pharmacokinetics and pharmacodynamics properties of a drug could be understood via study its mechanism of interaction with bovine serum albumin protein (BSA). Therefore, the interaction between MiADMSA with BSA was investigated using various spectroscopic techniques and computational methods. Linear quenching of BSA intrinsic fluorescence intensity with the … Show more

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Cited by 19 publications
(4 citation statements)
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“…Fluorescence spectroscopy is an important and useful technique for determining drug–protein interaction and providing information about drug association to proteins. , Various binding mechanism details on the binding site, binding affinity, and structural and conformational adaptations can be studied from fluorescence spectrophotometry studies. For the binding study of Mb with SMZ and SDZ, the excitation wavelength was examined at 295 nm, which selectively excites the emission maxima at 337 nm. The intrinsic fluorescence is mainly due to tyrosine (Tyr103, Tyr143, Tyr151) and tryptophan (Trp7, Trp14) residues present in Mb, which are subtle for the change in its microenvironment.…”
Section: Resultsmentioning
confidence: 99%
“…Fluorescence spectroscopy is an important and useful technique for determining drug–protein interaction and providing information about drug association to proteins. , Various binding mechanism details on the binding site, binding affinity, and structural and conformational adaptations can be studied from fluorescence spectrophotometry studies. For the binding study of Mb with SMZ and SDZ, the excitation wavelength was examined at 295 nm, which selectively excites the emission maxima at 337 nm. The intrinsic fluorescence is mainly due to tyrosine (Tyr103, Tyr143, Tyr151) and tryptophan (Trp7, Trp14) residues present in Mb, which are subtle for the change in its microenvironment.…”
Section: Resultsmentioning
confidence: 99%
“…Male rats treated with oral MiADMSA (25, 50, and 100 mg/kg showed moderate congestion, hemorrhage and infiltration of mononuclear cells, which caused inflammation, which is a defensive mechanism of the cells. All the changes, which were observed in the liver and kidney, were reversible in nature . Female rats, on the other hand, showed few signs of toxicity in liver and kidneys particularly at the higher dose level while no significant change was observed in the brain variables except for a significant decrease in the thiobarbituric reactive acid reactive substance levels at the lower dose 25 mg/kg.…”
Section: Toxicity (Safety Profile) Of Miadmsamentioning
confidence: 80%
“…All the changes, which were observed in the liver and kidney, were reversible in nature. 116 Female rats, on the other hand, showed few signs of toxicity in liver and kidneys particularly at the higher dose level while no significant change was observed in the brain variables except for a significant decrease in the thiobarbituric reactive acid reactive substance levels at the lower dose 25 mg/kg. No gross pathological changes were observed in these animals.…”
Section: Toxicity (Safety Profile) Of Miadmsamentioning
confidence: 88%
“…BSA is composed of a single polypeptide chain of 583 amino acid residues [46] and three domains named I, II, and III, each of which is divided into two subdomains (A and B) [47]. Studies indicate that the main association sites are located in the hydrophobic cavities of the IIA and IIIA subdomains [48]. The BSA structure has two Trp residues, Trp-134 in the first domain, located on the surface of the molecule, and Trp-212 in the IIA subdomain, located in the hydrophobic region of the protein [49,50].…”
Section: Bsa Binding Studymentioning
confidence: 99%