Fluorescence Interaction and Determination of Sulfathiazole with Trypsin

Gökoğlu, Elmas; Yılmaz, Ekrem

doi:10.1007/s10895-014-1427-7

Cited by 21 publications

(9 citation statements)

References 32 publications

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“…35 The quench of these two peaks suggests that the interaction of CAT with FW200 led slight unfolding of the polypeptides of CAT and resulted in a change of the protein structure which play an important role in keeping the catalytic activity of the enzyme. 36 This phenomenon conrmed the negative effects caused by FW200 to CAT and was in good accordance with the results of the uorescence measurement and UV-vis experiment.…”

Section: D Analysissupporting

confidence: 86%

Characterizing the binding interaction between ultrafine carbon black (UFCB) and catalase: electron microscopy and spectroscopic analysis

Zhang

Liu

2017

RSC Adv.

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Section: D Analysissupporting

confidence: 86%

Characterizing the binding interaction between ultrafine carbon black (UFCB) and catalase: electron microscopy and spectroscopic analysis

Zhang

Liu

2017

RSC Adv.

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“…Given that MET‐induced HSA fluorescence quenching is a static process, the binding constant ( K ) and the number of complexes bound to HSA ( n ) are determined by plotting the double‐logarithm regression curve of the fluorescence data through the following “modified” Stern–Volmer equation:

log false(F_{0} - F false) / F = log K + n log false[normalQ false]

where K is the binding constant of the site and n is the binding site multiplicity per binding site class. The results are summarized in Table .…”

Section: Resultsmentioning

confidence: 99%

“…Given that MET-induced HSA fluorescence quenching is a static process, the binding constant (K) and the number of complexes bound to HSA (n) are determined by plotting the double-logarithm regression curve of the fluorescence data through the following "modified" Stern-Volmer equation [48][49][50] : Table 3.…”

Section: Binding Modementioning

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

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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.

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“…AutoDock 4.2.6 was used to study the molecular docking of Mobic and PPL, and genetic algorithm was used to calculate the binding conformation of Mobic and PPL. [10] 3 Results and discussion…”

Section: Molecular Dockingmentioning

confidence: 99%

Spectroscopic and molecular docking studies on the binding mechanism of Mobic and lipase

Liu

Cheng

Zhang

2019

J Pharm Biopharm Res

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Under simulated physiological conditions (pH=7.40), the interaction between non-steroidal anti-inflammatory drug Mobic and lipase was studied by fluorescence spectra, ultraviolet absorption spectra, circular dichroism spectra and computer simulation technique. The experimental results showed that Mobic could quench the fluorescence of lipase by static quenching, and the binding site number is about 1. According to Förster's theory of non-radiation energy transfer, the binding distance between Mobic and lipase was obtained, r<7 nm, which indicated that there was non-radiation energy transfer in the system. The thermodynamic parameters were obtained from van't Hoff equation, Gibbs free energy ∆G<0, indicating that the reaction between them was spontaneous, ∆H<0, ∆S>0, indicating that hydrophobic force played a major role in the formation of Mobic and lipase complex. The results of synchronous fluorescence spectra, UV spectra and circular dichroism spectra showed that Mobic changed the conformation of lipase. The molecular docking results showed that the binding position of Mobic was close to the active center, indicating that Mobic could change the microenvironment of amino acid residues at the active center of lipase catalysis. The results of docking showed that there was hydrogen bond between Mobic and lipase, so the interaction between Mobic and lipase was driven by hydrophobic interaction and hydrogen bond.

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Fluorescence Interaction and Determination of Sulfathiazole with Trypsin

Cited by 21 publications

References 32 publications

Characterizing the binding interaction between ultrafine carbon black (UFCB) and catalase: electron microscopy and spectroscopic analysis

Characterizing the binding interaction between ultrafine carbon black (UFCB) and catalase: electron microscopy and spectroscopic analysis

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

Spectroscopic and molecular docking studies on the binding mechanism of Mobic and lipase

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