Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study

Rabbani, Gulam; Baig, Mohammad Hassan; Jan, Arif Tasleem; Lee, Eun Ju; Khan, Rizwan Hasan; Zaman, Masihuz; Farouk, Abd‐ElAziem

doi:10.1016/j.ijbiomac.2017.04.051

Cited by 207 publications

(68 citation statements)

References 39 publications

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“…As indicated by the authors, the second step “may play a crucial if not predominant role in determining the thermodynamics of protein association.” As this sentence implies, there must be cases where the first step is dominant, even though hydrogen bonds are involved. This was the case of G8 and ascorbyl palmitate, but there are many other examples in the literature …”

Section: Resultsmentioning

confidence: 99%

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest com-

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Section: Resultsmentioning

confidence: 99%

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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“…The Stern‐Volmer quenching constants ( K SV ), quenching constant ( k q ), and binding stoichiometry ( n ) at 298 K were calculated for CUM‐BSA and CUM‐HSA complexes and are summarized in Table . It is well known that the maximum scattering collision quenching constant k q of various quenchers with macromolecules is about 2.0 × 10 10 L mol −1 s −1 . Accordingly, k q (quenching constant) values for all participants were more than 2.0 × 10 10 L mol −1 s −1 .…”

Section: Resultsmentioning

confidence: 86%

“…On successive addition of CUMs from 0 to 120 μM concentration at constant concentration of protein (15 μM), tryptophan fluorescence intensity of BSA and HSA decreased gradually. It indicated that coumarin binding site is close to the tryptophan …”

Section: Resultsmentioning

confidence: 89%

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Sharma

Yadav

Sharma

et al. 2020

J of Molecular Recognition

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The interaction of triazole substituted 4-methyl-7-hydroxycoumarin derivatives (CUM1-4) with serum albumin (bovine serum albumin [BSA] and human serum albumin[HSA]) have been studied employing ultraviolet-visible (UV-Vis), fluorescence, circular dichroism (CD) spectroscopy, and molecular docking methods at physiological pH 7.4.The fluorescence quenching occurred with increasing concentration of CUMs, and the binding constant of CUM derivatives with BSA and HSA obtained from fluorescence quenching experiment was found to be~10 4 L mol −1 . CD study showed conformational changes in the secondary structure of serum albumin upon titration of CUMs.The observed experimental results were further validated by theoretical studies involving density functional theory (DFT) and molecular docking. K E Y W O R D S circular dichroism, coumarin, fluorescence quenching, molecular docking, serum albumin

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“…It is known that the α-helix is relevant to the hydrophobic property, the conversions of α-helix to β-sheet structures can occur by the insertion of aurantio-obtusin molecules into the hydrophobic surface of HSA, and the interaction enhanced the solvation effect between HSA and the water molecules, causing the protein side chains to associate with water molecules by hydrogen bonding and Van der Waals forces, decreasing the percentage of α-helix. [51][52][53] Some changes in the microenvironment around the HSA fluorophore can be reflected through the time-resolved fluorescence.…”

Section: Conformational Studiesmentioning

confidence: 99%

Investigation of the interaction of aurantio‐obtusin with human serum albumin by spectroscopic and molecular docking methods

et al. 2017

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The interaction between human serum albumin (HSA) and aurantio-obtusin was investigated by spectroscopic techniques combined with molecular docking. The Stern-Volmer quenching constants (K ) decreased from 8.56 × 10 M to 5.13 × 10 M with a rise in temperatures from 289 to 310 K, indicating that aurantio-obtusin produced a static quenching of the intrinsic fluorescence of HSA. Time-resolved fluorescence studies proved again that the static quenching mechanism was involved in the interaction. The sign and magnitude of the enthalpy change as well as the entropy change suggested involvement of hydrogen bonding and hydrophobic interaction in aurantio-obtusin-HSA complex formation. Aurantio-obtusin binding to HSA produced significant alterations in secondary structures of HSA, as revealed from the time-resolved fluorescence, Fourier transform infrared (FT-IR) spectroscopy, three-dimensional (3D) fluorescence and circular dichroism (CD) spectral results. Molecular docking study and site marker competitive experiment confirmed aurantio-obtusin bound to HSA at site I (subdomain IIA).

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Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study

Cited by 207 publications

References 39 publications

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Investigation of the interaction of aurantio‐obtusin with human serum albumin by spectroscopic and molecular docking methods

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