Fungicide methyl thiophanate binding at sub-domain IIA of human serum albumin triggers conformational change and protein damage

Saquib, Quaiser; Al-Khedhairy, Abdulaziz A.; Alarifi, Saud; Dwivedi, Sourabh; Mustafa, Jamal; Musarrat, Javed

doi:10.1016/j.ijbiomac.2010.03.020

Cited by 30 publications

(7 citation statements)

References 51 publications

(56 reference statements)

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“…There is a decrease in K q values with increasing temperature (Table ). The maximum scatter collision quenching constant (K q ) for various kinds of quenchers with biopolymer is approximately 2 × 10 10 L mol −1 s −1 . Thus, the K q values obtained in this case are of higher degree as compared with that in scatter mechanism.…”

Section: Resultsmentioning

confidence: 99%

Investigating the interaction of anticancer drug temsirolimus with human transferrin: Molecular docking and spectroscopic approach

Shamsi

Ahmed

Khan

et al. 2018

J of Molecular Recognition

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In our present study, binding between an important anti renal cancer drug temsirolimus and human transferrin (hTF) was investigated employing spectroscopic and molecular docking approach. In the presence of temsirolimus, hyper chromaticity is observed in hTF in UV spectroscopy suggestive of complex formation between hTF and temsirolimus. Fluorescence spectroscopy revealed the occurrence of quenching in hTF in the presence of temsirolimus implying complex formation taking place between hTF and temsirolimus. Further, the mode of interaction between hTF and temsirolimus was revealed to be static by fluorescence quenching analysis at 3 different temperatures. Binding constant values obtained employing fluorescence spectroscopy depicts strong interaction between hTF and temsirolimus; temsirolimus binds to hTF at 298 K with a binding constant of .32 × 10 M implying the strength of this interaction. The negative Gibbs free energy obtained through quenching experiments is evident of the fact that the binding is spontaneous. CD spectra of hTF also showed a downward shift in the presence of temsirolimus as compared with free hTF implying complex formation between hTF and temsirolimus. Molecular docking was performed with a view to find out which residues are key players in this interaction. The importance of our study stems from the fact it will provide an insight into binding pattern of commonly administered renal cancer drug with an important protein that plays a pivotal role in many physiological processes.

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Section: Resultsmentioning

confidence: 99%

Investigating the interaction of anticancer drug temsirolimus with human transferrin: Molecular docking and spectroscopic approach

Shamsi

Ahmed

Khan

et al. 2018

J of Molecular Recognition

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“…Synchronous uorescence spectra of HEWL were recorded using the same spectrophotometer at a wavelength interval (Dl) of 20 and 60 nm to probe, respectively, the microenvironment changes around the tyrosine (Tyr) and tryptophan (Trp) residues. [42][43][44] Three-dimensional uorescence spectra were recorded in the range of 200 to 600 nm. For extrinsic pyrene uorescence, the excitation was kept at 237 nm and emission was observed in the range of 350-450 nm.…”

Section: Fluorescence Measurementsmentioning

confidence: 99%

New insights into binding interaction of novel ester-functionalized m-E2-m gemini surfactants with lysozyme: a detailed multidimensional study

2015

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“…It also provides information about changes in the molecule environment in vicinity of the fluorophore functional group and is used to analyze protein samples. When the Δλ values between excitation and emission wavelengths were stabilized at 15‐20 nm or 60‐80 nm, synchronous fluorescence provided the characteristic information about tyrosine and tryptophan residues . In the present study, the synchronous fluorescence spectra of BSA at Δλ = 20 nm for tyrosine and Δλ = 80 nm for tryptophan are presented in Figures and , respectively.…”

Section: Resultsmentioning

confidence: 63%

Combining time‐resolved fluorescence with synchronous fluorescence spectroscopy to study bovine serum albumin‐curcumin complex during unfolding and refolding processes

Barakat

Patra

2012

Luminescence

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We investigated the complex interaction between bovine serum albumin (BSA) and curcumin by combining time-resolved fluorescence and synchronous fluorescence spectroscopy. The interaction was significant and sensitive to fluorescence lifetime and synchronous fluorescence characteristics. Binding of curcumin significantly shortened the fluorescence lifetime of BSA with a bi-molecular quenching rate constant of k(q) = 3.17 × 10(12) M(-1) s(-1). Denaturation by urea unfolded the protein molecule by quenching the fluorescence lifetime of BSA. The tyrosine synchronous fluorescence spectra were blue shifted whereas the position of tryptophan synchronous fluorescence spectra was red shifted during the unfolding process. However, denaturation of urea had little effect on the synchronous fluorescence peak of tyrosine in curcumin-BSA complex except in the low concentration range; however, it shifted the peak to the red, indicating that curcumin shifted tryptophan moiety to a more polar environment in the unfolded state. Decreases in the time-resolved fluorescence lifetime and curcumin-BSA complex during unfolding were recovered during refolding of BSA by a dilution process, suggesting partial reversibility of the unfolding process for both BSA and curcumin-BSA complex.

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Fungicide methyl thiophanate binding at sub-domain IIA of human serum albumin triggers conformational change and protein damage

Cited by 30 publications

References 51 publications

Investigating the interaction of anticancer drug temsirolimus with human transferrin: Molecular docking and spectroscopic approach

Investigating the interaction of anticancer drug temsirolimus with human transferrin: Molecular docking and spectroscopic approach

New insights into binding interaction of novel ester-functionalized m-E2-m gemini surfactants with lysozyme: a detailed multidimensional study

Combining time‐resolved fluorescence with synchronous fluorescence spectroscopy to study bovine serum albumin‐curcumin complex during unfolding and refolding processes

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