Experimental, computational and chemometrics studies of BSA-vitamin B6 interaction by UV–Vis, FT-IR, fluorescence spectroscopy, molecular dynamics simulation and hard-soft modeling methods

Manouchehri, Firouzeh; Izadmanesh, Yahya; Aghaee, Elham; Ghasemi, Jahan B.

doi:10.1016/j.bioorg.2016.07.014

Cited by 64 publications

(16 citation statements)

References 79 publications

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“…FT‐IR measurements can be used for finding the conformation of secondary structural changes occurred upon the binding of the drug to the macromolecule. Most investigations have focused on the amide I band that is highly responsive to the changes in secondary structure of the protein . In general, the peak positions in the spectral region 1600 to 1700 cm −1 of the amide protein I bands (mainly caused by C═O stretching vibration) are β‐sheet (1610‐1640 cm −1 ), random coil (1640‐1650 cm −1 ), α‐helix (1650‐1660 cm −1 ), β‐turn (1660‐1680 cm −1 ), and antiparalled β‐sheets (1680‐1690 cm −1 ), respectively .…”

Section: Resultsmentioning

confidence: 99%

“…In addition, there were 7 hydrogen bonds observed from the surrounding residues (Arg 198, Trp 213, Arg 217, His 241, Arg 256, and Glu 291). This finding also provided a good structural basis to explain the efficient fluorescence quenching of BSA upon fosinopril interaction . As evident from Table that van der Waals forces, hydrogen bonds and hydrophobic interactions contributed toward the stability of the fosinopril‐BSA complex, as the Δ E 2 was significantly more negative than Δ E 3 .…”

Section: Resultsmentioning

confidence: 99%

“…The docking results shown in Table 3 of BSA upon fosinopril interaction. 43 As evident from Table 3 that van der Waals forces, hydrogen bonds and hydrophobic interactions contributed toward the stability of the fosinopril-BSA complex, as the ΔE 2 was significantly more negative than ΔE 3 . These results were consistent with thermodynamic analysis and ANS binding assay experiments.…”

Section: Molecular Dockingmentioning

confidence: 93%

“…Most investigations have focused on the amide I band that is highly responsive to the changes in secondary structure of the protein. [41][42][43] In general, the peak positions in the spectral region 1600 to 1700 cm −1 of the amide protein I bands (mainly caused by C═O stretching vibration) are β-sheet (1610-1640 cm −1 ), random coil (1640-1650 cm −1 ), α-helix (1650-1660 cm −1 ), β-turn (1660-1680 cm −1 ), and antiparalled β-sheets (1680-1690 cm −1 ), respectively. 44 The FT-IR fitting curves of free BSA together with that of the protein in the complex were depicted in Figure 6A and 6B.…”

Section: Ft-ir Measurements For Secondary Structural Changesmentioning

confidence: 99%

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Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Zhou

Pan

Lou

et al. 2018

J of Molecular Recognition

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The intermolecular interaction of fosinopril, an angiotensin converting enzyme inhibitor with bovine serum albumin (BSA), has been investigated in physiological buffer (pH 7.4) by multi-spectroscopic methods and molecular docking technique. The results obtained from fluorescence and UV absorption spectroscopy revealed that the fluorescence quenching mechanism of BSA induced by fosinopril was mediated by the combined dynamic and static quenching, and the static quenching was dominant in this system. The binding constant, K , value was found to lie between 2.69 × 10 and 9.55 × 10 M at experimental temperatures (293, 298, 303, and 308 K), implying the low or intermediate binding affinity between fosinopril and BSA. Competitive binding experiments with site markers (phenylbutazone and diazepam) suggested that fosinopril preferentially bound to the site I in sub-domain IIA on BSA, as evidenced by molecular docking analysis. The negative sign for enthalpy change (ΔH ) and entropy change (ΔS ) indicated that van der Waals force and hydrogen bonds played important roles in the fosinopril-BSA interaction, and 8-anilino-1-naphthalenesulfonate binding assay experiments offered evidence of the involvements of hydrophobic interactions. Moreover, spectroscopic results (synchronous fluorescence, 3-dimensional fluorescence, and Fourier transform infrared spectroscopy) indicated a slight conformational change in BSA upon fosinopril interaction.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Molecular Dockingmentioning

confidence: 93%

Section: Ft-ir Measurements For Secondary Structural Changesmentioning

confidence: 99%

See 2 more Smart Citations

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Zhou

Pan

Lou

et al. 2018

J of Molecular Recognition

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“…The tyrosine residue (Tyr‐263) is also located in subdomain IIA . Due to their location, these fluorophore residues are easily assessable for ligand interaction and therefore play an important role in ligand–protein interaction …”

Section: Introductionmentioning

confidence: 99%

Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

et al. 2018

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The effect of a potent antimicrobial compound bearing 1,2,3-triazole core and a tryptophan tail, triazole-tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time-resolved fluorescence spectra further confirmed the involvement of static quenching for TTH-BSA system. The calculated thermodynamic parameters; ΔH, ΔS, and ΔG showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three-dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH-BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH-BSA binding.

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Spectroscopic investigation and structural simulation in human serum albumin with hydroxychloroquine/Silybum marianum and a possible potential COVID‐19 drug candidate

Tekyeh,

Shushtarian,

Bakhsh

et al. 2024

Archiv der Pharmazie

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In this study, the interaction between human serum albumin (HSA) and the hydroxychloroquine/Silybum marianum (HCQ/SM) mixture was investigated using various techniques. The observed high binding constant (Kb) and Stern–Volmer quenching constant (KSV) indicate a strong binding affinity between the HCQ/SM mixture and HSA. The circular dichroism (CD) analysis revealed that HCQ/SM induced conformational changes in the secondary structure of HSA, leading to a decrease in the α‐helical content. UV‐Vis analysis exhibited a slight redshift, indicating that the HCQ/SM mixture could adapt to the flexible structure of HSA. The experimental results demonstrated the significant conformational changes in HSA upon binding with HCQ/SM. Theoretical studies were carried out using molecular dynamics simulation via the Gromacs simulation package to explore insights into the drug interaction with HSA‐binding sites. Furthermore, molecular docking studies demonstrated that HCQ/SM‐HSA exhibited favorable docking scores with the receptor (5FUZ), suggesting a potential therapeutic relevance in combating COVID‐19 with a value of −6.24 kcal mol−1. HCQ/SM exhibited stronger interaction with both SARS‐CoV‐2 virus main proteases compared to favipiravir. Ultimately, the experimental data and molecular docking analysis presented in this research offer valuable insights into the pharmaceutical and biological properties of HCQ/SM mixtures when interacting with serum albumin.

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Experimental, computational and chemometrics studies of BSA-vitamin B6 interaction by UV–Vis, FT-IR, fluorescence spectroscopy, molecular dynamics simulation and hard-soft modeling methods

Cited by 64 publications

References 79 publications

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

Spectroscopic investigation and structural simulation in human serum albumin with hydroxychloroquine/Silybum marianum and a possible potential COVID‐19 drug candidate

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