Concentration-dependent antagonistic persuasion of SDS and naphthalene derivatives on the fibrillation of stem bromelain

Qadeer, Atiyatul; Ahmad, Ejaz; Zaman, Masihuz; Khan, Mohd Wasif; Khan, Javed Masood; Rabbani, Gulam; Tarique, K.F.; Sharma, Gaurav; Gourinath, S.; Nadeem, Sajid; Badr, Gamal; Khan, Rizwan Hasan

doi:10.1016/j.abb.2013.10.015

Cited by 35 publications

(16 citation statements)

References 53 publications

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“…Upon determination of binding mechanism, the values for K b and n were calculated according to Equation , from the intercept on y‐axis and the slope value of the graph plotted for log [( F o ‐ F )/ F ] vs log [ Q ] as depicted in Figure B and the values are listed in Table . The values of K b are inversely related to temperature implying that high temperature results in the formation less stable BSA‐TFB complex . The value for n was determined to be approximately equal to unity suggesting one independent site for binding of TFB on BSA.…”

Section: Resultsmentioning

confidence: 99%

A biophysical and computational study unraveling the molecular interaction mechanism of a new Janus kinase inhibitor Tofacitinib with bovine serum albumin

Nusrat

Ajmal

Zakariya

et al. 2016

J of Molecular Recognition

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The interaction of a recently certified kinase inhibitor Tofacitinib (TFB) with bovine serum albumin (BSA) has been studied, by spectroscopic and molecular docking studies. Spectrofluorimetric measurements at 3 different temperatures (288, 298, and 310 K) showed that TFB quench the intrinsic fluorescence of BSA upon forming a nonfluorescent complex. The intrinsic fluorescence data showed that TFB binds to BSA with binding constant (K ) of approximately 10 M , affirming a significant affinity of TFB with BSA. The decrease in Stern-Volmer quenching constant with increasing temperature exhibited the static mechanism of quenching. Negative value of ΔG (-6.94 ± 0.32 kcal·mol ), ΔH (-7.87 ± 0.52 kcal·mol ), and ΔS (-3.14 ± 0.42 cal·mol ·K ) at all 3 temperatures declared the reaction between BSA and TFB to be spontaneous and exothermic. Far-UV circular dichroism spectroscopy results demonstrated an increase in helical content of BSA in the presence of TFB. Moreover, dynamic light scattering measurements showed that TFB resulted into a decrease in the hydrodynamic radii (from 3.6 ± 0.053 to 2.9 ± 0.02 nm) of BSA. Molecular docking studies confirmed that TFB binds near site II on BSA, hydrogen bonding, and hydrophobic interaction were involved in the BSA-TFB complex formation. The present study characterizing the BSA-TFB interaction could be significant towards gaining an insight into the drug pharmacokinetics and pharmacodynamics and also in the direction of rational drug designing with better competence, against emerging immune-mediated diseases, ie, alopecia and rheumatoid arthritis.

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Section: Resultsmentioning

confidence: 99%

A biophysical and computational study unraveling the molecular interaction mechanism of a new Janus kinase inhibitor Tofacitinib with bovine serum albumin

Nusrat

Ajmal

Zakariya

et al. 2016

J of Molecular Recognition

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“…4). In the presence of 750 M taurine at 25 • C negative MRE value get increased which illustrated that taurine effectively stabilized the secondary structure of protein and it is well reported fact that secondary structure stabilizing elements are good inhibitor in amyloidogenic processes [27]. With the progress of incubation at 65 • C, secondary structural transition from ␣-helix to ␤-sheet start and after completion of aggregation process the CD spectra indicated the concomitant increase in ␤ sheet structure rather than ␣-helix [44].…”

Section: Effect Of Taurine On Secondary Structural Changes During Fibmentioning

confidence: 89%

“…Taurine is a small molecule containing amino as well as sulphonic group at both ends (inset of Fig. 1B), respectively so both of these groups have their own potential to disrupt the interaction formed during the fibrillation process [27,[39][40][41]. Table 2 Parameters obtained from fitting the turbidity and ThT fluorescence data obtained for inhibition of HSA aggregation by taurine.…”

Section: Inhibitory Effect Of Taurine On Hsa Fibril Formation As Monimentioning

confidence: 98%

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Biophysical insight into the anti-amyloidogenic behavior of taurine

Chaturvedi

Alam

Khan

et al. 2015

International Journal of Biological Macromolecules

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“…The predicted profile of titration of charge as a function of pH for all five hyperthermophile-derived P. furiosus proteins, and for T. maritima PEPM50, is shown in SupplementaryFigure S4. Earlier, it has been reported that some mesophile-derived proteins (lysozyme and stem bromelain) form amyloids in the SDS concentration range of 0.5-1.0 mM SDS, and that fibril formation is suppressed at higher concentrations44 . In the case of lysozyme, in the pH range of 4.0-1.0, amyloid formation was found to be induced in the broader concentration range of 0.1-2.5 mM SDS, presumably owing to lysozyme having a higher net positive charge at pH 7.0, in comparison to what obtains at pH 7.0 49 .…”

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confidence: 99%

The Achilles’ Heel of “Ultrastable” Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in Proteins Carrying Overall Positive Charge

et al. 2016

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Low concentrations (<3.0 mM) of the anionic surfactant sodium dodecyl sulfate (SDS) have been shown to induce the formation of amyloid fibers in more than 20 different mesophile-derived proteins in the cationic state. It is not known whether SDS has similar effects on hyperthermophile-derived proteins, which are otherwise thought to be "ultrastable" and inordinately resistant to structural perturbations at room temperature. Here, we show that low (<4.5 mM) concentrations of SDS rapidly induce the formation of aggregates and amyloid fibers in five different ultrastable Pyrococcus furiosus proteins in the cationic state. We also show that amyloid formation is accompanied by the development of a characteristic, negative circular dichroism band at ∼230 nm. These effects are not seen if the proteins have a net negative charge or when higher concentrations of SDS are used (which induce helix formation instead). Our results appear to reveal a potential weakness or "Achilles' heel" in ultrastable proteins from hyperthermophiles. They also provide very strong support for the view that SDS initially interacts with proteins through electrostatic interactions, and not hydrophobic interactions, eliciting similar effects entirely regardless of protein molecular weight, or structural features such as quaternary structure or tertiary structural stability.

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Concentration-dependent antagonistic persuasion of SDS and naphthalene derivatives on the fibrillation of stem bromelain

Cited by 35 publications

References 53 publications

A biophysical and computational study unraveling the molecular interaction mechanism of a new Janus kinase inhibitor Tofacitinib with bovine serum albumin

A biophysical and computational study unraveling the molecular interaction mechanism of a new Janus kinase inhibitor Tofacitinib with bovine serum albumin

Biophysical insight into the anti-amyloidogenic behavior of taurine

The Achilles’ Heel of “Ultrastable” Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in Proteins Carrying Overall Positive Charge

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