Molecular modeling and multispectroscopic studies of the interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin

Shahabadi, Nahid; Falsafi, Monireh; Hadidi, Saba

doi:10.1016/j.jlumin.2015.07.006

Cited by 13 publications

(7 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Meanwhile, for dynamic quenching, the maximum K q of various quenchers with biopolymers, which reflects the efficiency of quenching or the accessibility of the fluorophores to the quencher, is 2.0 × 10 10 L mol −1 seconds −1. In this study, Stern‐Volmer plots of TF–pepsin and trypsin at different temperatures are shown in Figure . Good linearity within the investigated concentrations was observed.…”

Section: Resultsmentioning

confidence: 99%

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

Huang

et al. 2016

J of Molecular Recognition

View full text Add to dashboard Cite

Tolvaptan (TF), a selective arginine vasopressin V2 receptor antagonist, was approved by the Food and Drug Administration in 2009. This study mainly investigated the differences between the binding of TF with pepsin and trypsin by using a series of spectroscopy and molecular modeling methods. Thermodynamic parameters and molecular docking results suggested that the binding of TF to pepsin and trypsin were both spontaneous but driven by different forces. For pepsin, the binding was driven by hydrogen bonds and van der Waals forces; but for trypsin, it was driven by electrostatic forces and hydrophobic forces. The quenching mechanism between TF and pepsin and trypsin was investigated by fluorescence experiments and time-resolved fluorescence spectroscopy. Synchronous fluorescence and 3-dimensional fluorescence were used to investigate the micro-environmental and conformational changes of pepsin and trypsin after the insertion of TF. In addition, activity-measurement results showed that both the pepsin and trypsin activities increased with increasing TF concentration, which may help to understand the possible effect of TF on the digestion and absorption of nutrients in vivo.

show abstract

Section: Resultsmentioning

confidence: 99%

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

Huang

et al. 2016

J of Molecular Recognition

View full text Add to dashboard Cite

show abstract

“…It is imperative to believe structural alterations in the protein consequent to ligand binding. In many ligand binding studies, changes in the protein's structures (secondary or tertiary or both) together with microenvironmental alterations around protein fluorophores have been reported . HSA has been categorized as a helical protein due to the presence of 67% α‐helical structure .…”

Section: Discussionmentioning

confidence: 99%

“…In many ligand binding studies, changes in the protein's structures (secondary or tertiary or both) together with microenvironmental alterations around protein fluorophores have been reported. [59][60][61] HSA has been categorized as a helical protein due to the presence of 67% α-helical structure. [10] Helical structure of the protein was apparent from the presence of minima (208 and 222 nm) in the 200-250 nm region of the CD spectra ( Figure 3A).…”

Section: Discussionmentioning

confidence: 99%

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

et al. 2019

View full text Add to dashboard Cite

The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF‐HSA interaction were found to fall within the range of 3.79‐5.73 × 104 M˗1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF‐HSA complex, as deduced from the thermodynamic data (ΔS = +133.52 J mol−1 K−1 and ΔH = +13.09 kJ mol−1) of the binding reaction and molecular docking analysis. Three‐dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200‐250 and 250‐300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis.

show abstract

“…where F 0 and F are the fluorescence intensities in the absence and presence of the quencher, respectively, and K SV is the Stern-Volmer quenching constant (represented by K D if quenching is dynamic). [27][28][29] based on complex formation. [30][31][32] Fluorescence lifetime measurements can distinguish static quenching from dynamic quenching.…”

Section: Fluorescence Quenching Measurementsmentioning

confidence: 99%

The binding properties of metandienone and human serum albumin by comparing with other five similar compounds

Lin

Wang

Peng

et al. 2016

J Biochem & Molecular Tox

View full text Add to dashboard Cite

Metandienone (MET) is an exogenous anabolic androgenic steroid. The interaction between MET and human serum albumin (HSA) was investigated by molecular modeling and different optical techniques. There was no possibility of energy transfer, and the fluorescence quenching of HSA induced by MET was mainly due to the complex formation. The differences of binding ability between MET and compounds 1-5 were significantly caused by space steric hindrance. The single crystallographic data of two steroids (compounds 4 and 5) were obtained in the methanol at the first time. In addition, the binding ability was slightly affected by -OH, -CH , and -COCH . The results of displacement experiment demonstrated that the MET binding site was mainly located in site 1 of HSA. H-bonding and van der Waals forces were significant in the MET-HSA binding. MET played an insignificant role on the local conformation change in HSA.

show abstract

Molecular modeling and multispectroscopic studies of the interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin

Cited by 13 publications

References 41 publications

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

The binding properties of metandienone and human serum albumin by comparing with other five similar compounds

Contact Info

Product

Resources

About