Displaying all 15 publications

Abstract:
Sort:
  1. Spectroscopic studies on the binding of bromocresol purple to different serum albumins and its bilirubin displacing action
    Faizul FM, Abdul Kadir H, Tayyab S
    J. Photochem. Photobiol. B, Biol., 2008 Jan 30;90(1):1-7.
    PMID: 18024146
    The interaction between bromocresol purple (BCP) and bovine serum albumin (BSA)/porcine serum albumin (PSA) was investigated both in the absence and presence of bilirubin (BR) using absorption/absorption difference spectroscopy. A significant red shift in the absorption maxima of BCP accompanied by a decrease in absorbance was indicative of BCP binding to albumin. The titration of BSA and PSA with BCP using absorption difference spectroscopy and analysis of results by Benesi-Hildebrand equation yielded the values of association constant, K as 9.9+/-0.9x10(4)Lmol(-1) and 4.1+/-0.3x10(4)Lmol(-1) for BSA and PSA, respectively. The differential extinction coefficient (Deltaepsilon) of 34,484M(-1)cm(-1) at 615nm and 41,870M(-1)cm(-1) at 619nm were estimated for BSA and PSA, respectively. Decrease in (DeltaAbs.)(615nm) of BCP-BSA complex with the increase in ionic strength suggested the role of hydrophobic interactions in the binding phenomenon. A significant blue shift in the absorption maxima and change in (DeltaAbs)(lambdamax) values of BR-albumin complexes upon addition of increasing concentrations of BCP revealed the BR displacing action of BCP on albumin molecule.
    Matched MeSH terms: Serum Albumin/chemistry*
  2. Fulltext Spectrofluorometric and molecular docking studies on the binding of curcumenol and curcumenone to human serum albumin
    Hamdi OA, Feroz SR, Shilpi JA, Anouar el H, Mukarram AK, Mohamad SB, et al.
    Int J Mol Sci, 2015;16(3):5180-93.
    PMID: 25756376 DOI: 10.3390/ijms16035180
    Curcumenol and curcumenone are two major constituents of the plants of medicinally important genus of Curcuma, and often govern the pharmacological effect of these plant extracts. These two compounds, isolated from C. zedoaria rhizomes were studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Additions of these sesquiterpenes to HSA produced significant fluorescence quenching and blue shifts in the emission spectra of HSA. Analysis of the fluorescence data pointed toward moderate binding affinity between the ligands and HSA, with curcumenone showing a relatively higher binding constant (2.46 × 105 M-1) in comparison to curcumenol (1.97 × 104 M-1). Cluster analyses revealed that site I is the preferred binding site for both molecules with a minimum binding energy of -6.77 kcal·mol-1. However, binding of these two molecules to site II cannot be ruled out as the binding energies were found to be -5.72 and -5.74 kcal·mol-1 for curcumenol and curcumenone, respectively. The interactions of both ligands with HSA involved hydrophobic interactions as well as hydrogen bonding.
    Matched MeSH terms: Serum Albumin/chemistry
  3. Fulltext Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
    Wong YH, Abdul Kadir H, Tayyab S
    ScientificWorldJournal, 2013;2013:981902.
    PMID: 24222758 DOI: 10.1155/2013/981902
    Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe. BSA was labelled with FITC using chemical coupling, and urea and thermal denaturation studies were performed on FITC-labelled BSA (FITC-BSA) both in the absence and presence of 10% and 20% (w/v) honey using FITC fluorescence at 522 nm upon excitation at 495 nm. There was an increase in the FITC fluorescence intensity upon increasing urea concentration or temperature, suggesting protein denaturation. The results from urea and thermal denaturation studies showed increased stability of protein in the presence of honey as reflected from the shift in the transition curve along with the start point and the midpoint of the transition towards higher urea concentration/temperature. Furthermore, the increase in ΔG D (H2O) and ΔG D (25°C) in presence of honey also suggested protein stabilization.
    Matched MeSH terms: Serum Albumin/chemistry*
  4. Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement
    Mathavan VM, Boh BK, Tayyab S
    Indian J. Biochem. Biophys., 2009 Aug;46(4):325-31.
    PMID: 19788065
    The interaction of crythrosine B (ErB), a commonly used dye for coloring foods and drinks, with bovine scrum albumin (BSA) was investigated both in the absence and presence of bilirubin (BR) using absorption and absorption difference spectroscopy. ErB binding to BSA was reflected from a significant red shift of 11 nm in the absorption maximum of ErB (527 nm) with the change in absorbance at lamdamax. Analysis of absorption difference spectroscopic titration results of BSA with increasing concentrations of ErB3 using Benesi-Hildebrand equation gave the association constant, K as 6.9 x 10(4) M(-1). BR displacing action of ErB was revealed by a significant blue shift in the absorption maximum, accompanied by a decrease in absorbance difference at lamdamax in the difference spectrum of BR-BSA complex upon addition of increasing concentrations of ErB. This was further substantiated by fluorescence spectroscopy, as addition of increasing concentrations of ErB to BR-BSA complex caused a significant decrease in fluoresccnce at 510 nm. The results suggest that ErB binds to a site in the vicinity of BR binding site on BSA. Therefore, intake of ErB may increase the risk of hyperbilirubinemia in the healthy subjects.
    Matched MeSH terms: Serum Albumin/chemistry
  5. Stabilization of Human Serum Albumin against Urea Denaturation by Diazepam and Ketoprofen
    Manoharan P, Wong YH, Tayyab S
    Protein Pept Lett, 2015;22(7):611-7.
    PMID: 25961707
    Stabilizing effect of diazepam and ketoprofen, Sudlow's site II markers on human serum albumin (HSA) against urea denaturation was studied using fluorescence spectroscopy. The two-step, three-state urea transition of HSA was transformed into a single-step, two-state transition with the abolishment of the intermediate state along with a shift of the transition curve towards higher urea concentrations in the presence of diazepam or ketoprofen. Interestingly, a greater shift in the transition curve of HSA was observed in the presence of ketoprofen compared to diazepam. A comparison of the intrinsic fluorescence and three-dimensional fluorescence spectra of HSA and partially-denatured HSAs, obtained in the absence and the presence of diazepam or ketoprofen suggested significant retention of native-like conformation in the partially-denatured states of HSA in the presence of Sudlow's site II markers. Taken together, all these results suggested stabilization of HSA in the presence of diazepam or ketoprofen, being greater in the presence of ketoprofen.
    Matched MeSH terms: Serum Albumin/chemistry*
  6. Exploring ligand-protein interaction: A laboratory exercise on herbicide binding to plasma transport protein
    Roslan AA, Tayyab S
    Biochem Mol Biol Educ, 2019 03;47(2):156-160.
    PMID: 30629781 DOI: 10.1002/bmb.21207
    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 (Ksv ) and bimolecular quenching rate constant (kq ), whereas values of the binding constant (Ka ) 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. © 2019 International Union of Biochemistry and Molecular Biology, 47(2): 156-160, 2019.
    Matched MeSH terms: Serum Albumin/chemistry*
  7. Fulltext Drug Delivery System for Refractory Cancer Therapy via an Endogenous Albumin Transport System
    Ishima Y, Maruyama T, Otagiri M, Ishida T
    Chem Pharm Bull (Tokyo), 2020;68(7):583-588.
    PMID: 32611995 DOI: 10.1248/cpb.c20-00026
    A unique phenomenon in solid tumors, the enhanced permeability and retention (EPR) effect is now well known in the development of macromolecular anticancer therapy. However, cancers with low vascular permeability have posed a challenge for these EPR based therapeutic systems. An intrinsic vascular modulator, such as nitric oxide (NO), could augment the endogenous EPR effect. However, the most important aim has been to construct an effective NO delivery system for cancer. Since it is well known that human serum albumin is one of the most important endogenous NO transport proteins in human circulation, for more than a decade we have demonstrated that S-nitrosated human serum albumin dimer (SNO-HSA-Dimer) becomes an enhancer of the EPR effect. Here, we summarize the enhanced effect of SNO-HSA-Dimer on the anticancer effect of macromolecular anticancer drugs such as PEGylated liposomal doxorubicin (Doxil®). In C26-bearing mice with highly permeable vasculature, SNO-HSA-Dimer is able to increase more 3-fold the tumor accumulation of these anticancer drugs, thereby tripling their anticancer effects. Interestingly, the tumor accumulation of Doxil® in B16-bearing mice, which are characterized by a low permeable vasculature, increased more than 6-fold in the presence of SNO-HSA-Dimer, and the improved accumulation of Doxil® led to both increased survival and decreased tumor volume. These results strongly suggest that the more cancer is refractory, the more the SNO-HSA-Dimer could enhance the EPR effect via an endogenous albumin transport (EAT) system. Accordingly, we conclude that the EAT system is promising as a drug delivery system (DDS) strategy for refractory cancer therapy.
    Matched MeSH terms: Serum Albumin/chemistry*
  8. Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies
    Tayyab S, Zaroog MS, Feroz SR, Mohamad SB, Malek SN
    Int J Pharm, 2015 Aug 1;491(1-2):352-8.
    PMID: 26142245 DOI: 10.1016/j.ijpharm.2015.06.042
    The interaction of tranilast (TRN), an antiallergic drug with the main drug transporter in human circulation, human serum albumin (HSA) was studied using isothermal titration calorimetry (ITC), fluorescence spectroscopy and in silico docking methods. ITC data revealed the binding constant and stoichiometry of binding as (3.21 ± 0.23) × 10(6)M(-1) and 0.80 ± 0.08, respectively, at 25°C. The values of the standard enthalpy change (ΔH°) and the standard entropy change (ΔS°) for the interaction were found as -25.2 ± 5.1 kJ mol(-1) and 46.9 ± 5.4 J mol(-1)K(-1), respectively. Both thermodynamic data and modeling results suggested the involvement of hydrogen bonding, hydrophobic and van der Waals forces in the complex formation. Three-dimensional fluorescence data of TRN-HSA complex demonstrated significant changes in the microenvironment around the protein fluorophores upon drug binding. Competitive drug displacement results as well as modeling data concluded the preferred binding site of TRN as Sudlow's site I on HSA.
    Matched MeSH terms: Serum Albumin/chemistry
  9. Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study
    Tayyab S, Izzudin MM, Kabir MZ, Feroz SR, Tee WV, Mohamad SB, et al.
    J. Photochem. Photobiol. B, Biol., 2016 Sep;162:386-94.
    PMID: 27424099 DOI: 10.1016/j.jphotobiol.2016.06.049
    Binding characteristics of a promising anticancer drug, axitinib (AXT) to human serum albumin (HSA), the major transport protein in human blood circulation, were studied using fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy as well as molecular docking analysis. A gradual decrease in the Stern-Volmer quenching constant with increasing temperature revealed the static mode of the protein fluorescence quenching upon AXT addition, thus confirmed AXT-HSA complex formation. This was also confirmed from alteration in the UV-vis spectrum of HSA upon AXT addition. Fluorescence quenching titration results demonstrated moderately strong binding affinity between AXT and HSA based on the binding constant value (1.08±0.06×10(5)M(-1)), obtained in 10mM sodium phosphate buffer, pH7.4 at 25°C. The sign and magnitude of the enthalpy change (∆H=-8.38kJmol(-1)) as well as the entropy change (∆S=+68.21Jmol(-1)K(-1)) clearly suggested involvement of both hydrophobic interactions and hydrogen bonding in AXT-HSA complex formation. These results were well supported by molecular docking results. Three-dimensional fluorescence spectral results indicated significant microenvironmental changes around Trp and Tyr residues of HSA upon complexation with AXT. AXT binding to the protein produced significant alterations in both secondary and tertiary structures of HSA, as revealed from the far-UV and the near-UV CD spectral results. Competitive drug displacement results obtained with phenylbutazone (site I marker), ketoprofen (site II marker) and hemin (site III marker) along with molecular docking results suggested Sudlow's site I, located in subdomain IIA of HSA, as the preferred binding site of AXT.
    Matched MeSH terms: Serum Albumin/chemistry*
  10. Impact of bovine and human serum albumin on Curcumin in vitro activity against Staphylococcus aureus
    Teow SY, Ali SA
    Pak J Pharm Sci, 2017 May;30(3):891-895.
    PMID: 28653935
    This study evaluated the impact of pH (7.4 and 6.5), bovine serum albumin (BSA), and human serum albumin (HSA) on Curcumin activity against 2 reference, 1 clinical, and 10 environmental strains of Staphylococcus aureus (S. aureus). Minimal inhibitory concentrations (MICs) of Curcumin against S. aureus were statistically indifferent (p>0.05) at pH7.4 and pH6.5. Activity of Curcumin against S. aureus was reduced by two folds in the presence of 1.25-5% BSA/HSA.
    Matched MeSH terms: Serum Albumin/chemistry
  11. Supramolecular interaction of 6-shogaol, a therapeutic agent of Zingiber officinale with human serum albumin as elucidated by spectroscopic, calorimetric and molecular docking methods
    Feroz SR, Mohamad SB, Lee GS, Malek SN, Tayyab S
    Phytomedicine, 2015 Jun 01;22(6):621-30.
    PMID: 26055127 DOI: 10.1016/j.phymed.2015.03.016
    BACKGROUND: 6-Shogaol, one of the main bioactive constituents of Zingiber officinale has been shown to possess various therapeutic properties. Interaction of a therapeutic compound with plasma proteins greatly affects its pharmacokinetic and pharmacodynamic properties.

    PURPOSE: The present investigation was undertaken to characterize the interaction between 6-shogaol and the main in vivo transporter, human serum albumin (HSA).

    METHODS: Various binding characteristics of 6-shogaol-HSA interaction were studied using fluorescence spectroscopy. Thermal stability of 6-shogaol-HSA system was determined by circular dichroism (CD) and differential scanning calorimetric (DSC) techniques. Identification of the 6-shogaol binding site on HSA was made by competitive drug displacement and molecular docking experiments.

    RESULTS: Fluorescence quench titration results revealed the association constant, Ka of 6-shogaol-HSA interaction as 6.29 ± 0.33 × 10(4) M(-1) at 25 ºC. Values of the enthalpy change (-11.76 kJ mol(-1)) and the entropy change (52.52 J mol(-1) K(-1)), obtained for the binding reaction suggested involvement of hydrophobic and van der Waals forces along with hydrogen bonds in the complex formation. Higher thermal stability of HSA was noticed in the presence of 6-shogaol, as revealed by DSC and thermal denaturation profiles. Competitive ligand displacement experiments along with molecular docking results suggested the binding preference of 6-shogaol for Sudlow's site I of HSA.

    CONCLUSION: All these results suggest that 6-shogaol binds to Sudlow's site I of HSA through moderate binding affinity and involves hydrophobic and van der Waals forces along with hydrogen bonds.

    Matched MeSH terms: Serum Albumin/chemistry*
  12. Conformational properties of serum albumin binding sites in rats with different behaviour in the open field test
    Gryzunov YA, Koplik EV, Smolina NV, Kopaeva LB, Dobretsov GE, Sudakov KV
    Stress, 2006 Mar;9(1):53-60.
    PMID: 16753933
    In this study, the hypothesis was tested that behaviour of rats under the open field test condition and effects of subsequent acute stress relate to conformational properties of the main plasma carrier protein, albumin.To evaluate albumin properties, fluorescence intensity of a molecular probe CAPIDAN (N-carboxyphenylimide of dimethylaminonaphthalic acid) at N (at pH 7.4) and F (at pH 4.2) albumin conformations was measured and the N-F signal ratio was calculated. The data obtained showed that CAPIDAN fluoresces selectively from albumin in rat serum and its fluorescence is sensitive to binding of fatty acids and some other ligands to albumin. Behaviour of 78 Wistar male rats was characterized from the fraction of time taken for exploratory and ambulatory activity during the open field test. In rats not subjected to stress (n = 40), a negative correlation was revealed between open field activity and CAPIDAN N-to-F ratio for albumin (r = - 0.55, p < 0.0005). In the group of rats subjected to acute stress (immobilization plus stochastic electrocutaneous stimulation) the correlation between behavioural activity and the albumin conformational properties was significantly positive (r = 0.59, p < 0.0001): the CAPIDAN albumin fluorescence ratio increased in the highly active rats and decreased in the low-activity rats. The mechanisms of the observed effects may involve differences in nonesterified fatty acid production during stress.
    Matched MeSH terms: Serum Albumin/chemistry*
  13. Characterization of the binding of an anticancer drug, lapatinib to human serum albumin
    Kabir MZ, Mukarram AK, Mohamad SB, Alias Z, Tayyab S
    J. Photochem. Photobiol. B, Biol., 2016 Jul;160:229-39.
    PMID: 27128364 DOI: 10.1016/j.jphotobiol.2016.04.005
    Interaction of a promising anticancer drug, lapatinib (LAP) with the major transport protein in human blood circulation, human serum albumin (HSA) was investigated using fluorescence and circular dichroism (CD) spectroscopy as well as molecular docking analysis. LAP-HSA complex formation was evident from the involvement of static quenching mechanism, as revealed by the fluorescence quenching data analysis. The binding constant, Ka value in the range of 1.49-1.01×10(5)M(-1), obtained at three different temperatures was suggestive of the intermediate binding affinity between LAP and HSA. Thermodynamic analysis of the binding data (∆H=-9.75kJmol(-1) and ∆S=+65.21Jmol(-1)K(-1)) suggested involvement of both hydrophobic interactions and hydrogen bonding in LAP-HSA interaction, which were in line with the molecular docking results. LAP binding to HSA led to the secondary and the tertiary structural alterations in the protein as evident from the far-UV and the near-UV CD spectral analysis, respectively. Microenvironmental perturbation around Trp and Tyr residues in HSA upon LAP binding was confirmed from the three-dimensional fluorescence spectral results. LAP binding to HSA improved the thermal stability of the protein. LAP was found to bind preferentially to the site III in subdomain IB on HSA, as probed by the competitive drug displacement results and supported by the molecular docking results. The effect of metal ions on the binding constant between LAP and HSA was also investigated and the results showed a decrease in the binding constant in the presence of these metal ions.
    Matched MeSH terms: Serum Albumin/chemistry
  14. Interaction of a tyrosine kinase inhibitor, vandetanib with human serum albumin as studied by fluorescence quenching and molecular docking
    Kabir MZ, Feroz SR, Mukarram AK, Alias Z, Mohamad SB, Tayyab S
    J Biomol Struct Dyn, 2016 Aug;34(8):1693-704.
    PMID: 26331959 DOI: 10.1080/07391102.2015.1089187
    Interaction of a tyrosine kinase inhibitor, vandetanib (VDB), with the major transport protein in the human blood circulation, human serum albumin (HSA), was investigated using fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking analysis. The binding constant of the VDB-HSA system, as determined by fluorescence quenching titration method was found in the range, 8.92-6.89 × 10(3 )M(-1) at three different temperatures, suggesting moderate binding affinity. Furthermore, decrease in the binding constant with increasing temperature revealed involvement of static quenching mechanism, thus affirming the formation of the VDB-HSA complex. Thermodynamic analysis of the binding reaction between VDB and HSA yielded positive ΔS (52.76 J mol(-1) K(-1)) and negative ΔH (-6.57 kJ mol(-1)) values, which suggested involvement of hydrophobic interactions and hydrogen bonding in stabilizing the VDB-HSA complex. Far-UV and near-UV CD spectral results suggested alterations in both secondary and tertiary structures of HSA upon VDB-binding. Three-dimensional fluorescence spectral results also showed significant microenvironmental changes around the Trp residue of HSA consequent to the complex formation. Use of site-specific marker ligands, such as phenylbutazone (site I marker) and diazepam (site II marker) in competitive ligand displacement experiments indicated location of the VDB binding site on HSA as Sudlow's site I (subdomain IIA), which was further established by molecular docking results. Presence of some common metal ions, such as Ca(2+), Zn(2+), Cu(2+), Ba(2+), Mg(2+), and Mn(2+) in the reaction mixture produced smaller but significant alterations in the binding affinity of VDB to HSA.
    Matched MeSH terms: Serum Albumin/chemistry*
  15. Enantiomeric pair of copper(II) polypyridyl-alanine complexes: Effect of chirality on their interaction with biomolecules
    Ng CH, Chan CW, Lai JW, Ooi IH, Chong KV, Maah MJ, et al.
    J Inorg Biochem, 2016 07;160:1-11.
    PMID: 27105312 DOI: 10.1016/j.jinorgbio.2016.04.003
    Like chiral organic drugs, the chemical and biological properties of metal complexes can be dependent on chirality. Two pairs of [Cu(phen)(ala)(H2O)]X·xH2O (phen=1.10-phenanthroline: X=NO3(-); ala: l-alanine (l-ala), 1 and d-alanine (d-ala) 2; and (X=Cl(-); ala: l-ala, 3 and d-ala, 4) complex salts (x=number of lattice water molecules) have been synthesized and characterized. The crystal structure of 3 has been determined. The same pair of enantiomeric species, viz. [Cu(phen)(l-ala)(H2O)](+) and [Cu(phen)(d-ala)(H2O)](+), have been identified to be present in the aqueous solutions of both 1 and 3, and in those of both 2 and 4 respectively. Both 3 and 4 bind more strongly to ds(AT)6 than ds(CG)6. There is no or insignificant effect of the chirality of 3 and 4 on the production of hydroxyl radicals, binding to deoxyribonucleic acid from calf thymus (CT-DNA), ds(CG)6, G-quadruplex and 17-base pair duplex, and inhibition of both topoisomerase I and proteasome. Among the three proteasome proteolytic sites, the trypsin-like site is inhibited most strongly by these complexes. However, the chirality of 3 and 4 does affect the number of restriction enzymes inhibited, and their binding constants towards ds(AT)6 and serum albumin.
    Matched MeSH terms: Serum Albumin/chemistry
Related Terms
Filters
Contact Us

Please provide feedback to Administrator ([email protected])

External Links