Spectroscopic investigations on the interactions between isopropanol and trypsin at molecular level

Hu, Xinxin; Zhang, Yu; Liu, Rutao

doi:10.1016/j.saa.2013.01.072

Cited by 80 publications

(34 citation statements)

References 29 publications

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“…Trypsin is a globular protein with a medium size and 223 amino acid residues 15 . Enzyme has two domains, each of which consists of 6 anti-parallel polypeptide chains.…”

Section: Methodsmentioning

confidence: 99%

“…Only Trp 51, because of being relatively away from cysteine residues, can be involved in the overall fluorescence emission 15,30 . Tryptophan close to cysteine cannot significantly participate in the fluorescence emission.…”

Section: Fluorescence Spectroscopymentioning

confidence: 99%

“…The α-helix and β-sheet contents of trypsin were changed together 15,46 . The α-helix and β-sheet contents of trypsin were changed together 15,46 .…”

Section: Measurementsmentioning

confidence: 99%

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The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

et al. 2016

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This work studied the interaction between spermine and trypsin at pH 8.0. The thermal stability of trypsin was investigated in the presence of spermine over a temperature range (from 293 K to 353 K).Additionally, the conformational change of trypsin induced by spermine was analyzed by UV-Vis absorption and fluorescence spectra. The effect of spermine on trypsin activity was studied at 37 °C and pH 8.0, using Tris-HCl as a buffer. The fluorescence spectroscopy results indicated that the binding of spermine to trypsin was a spontaneous binding process. The fluorescence of trypsin was quenched by spermine through the static quenching mechanism. By increasing the concentration of spermine, the thermal stability of trypsin was increased. The quantitative analysis of CD spectra revealed some information regarding the changes in the content of the α-helix and the β-sheet of the trypsin upon binding to spermine. It was also found that by increasing the concentration of spermine, the activity of 2 trypsin was increased. Molecular docking results also revealed the presence of one binding site with a negative value for the Gibbs free energy of the binding of spermine to trypsin. Further, the docking and fluorescence spectroscopy study revealed that van der Waals interactions and hydrogen bonds played a major role in stabilizing the complex. As a result, spermine could be considered as an activator and stabilizer for trypsin.

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“…Trypsin is a globular protein with a medium size and 223 amino acid residues 15 . Enzyme has two domains, each of which consists of 6 anti-parallel polypeptide chains.…”

Section: Methodsmentioning

confidence: 99%

Section: Fluorescence Spectroscopymentioning

confidence: 99%

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The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

et al. 2016

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“…Its catalytic site consists of one catalytic triad composed by His57, Asp102 and Ser195, responsible for the hydrolysis of C-terminal side of lysine and arginine as well as amide linkages and ester of substrates. Due to its essential physiological function, it has often been chosen as target protein to study the structural effects of small molecules to trypsin and thereby the function [27][28][29][30]. However, there still lacks studies on the interactions of TBBPA and TBBPS with bovine trypsin.…”

Section: Introductionmentioning

confidence: 99%

Atomic-scale investigation of the interactions between tetrabromobisphenol A, tetrabromobisphenol S and bovine trypsin by spectroscopies and molecular dynamics simulations

Ding

Zhang

Wang

et al. 2015

Journal of Hazardous Materials

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“…Trypsin consists of 223 amino residues with a molecular mass of 23,300 Da [2]. It contains two domains of nearly equal size, and each domain comprises a set of six antiparallel strands of polypeptide chain laced together into a b-sheet unit by a network of H-bonds [3,4].…”

Section: Introductionmentioning

confidence: 99%

Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies

Liu

Zhang

Liao

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Spectroscopic investigations on the interactions between isopropanol and trypsin at molecular level

Cited by 80 publications

References 29 publications

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

Atomic-scale investigation of the interactions between tetrabromobisphenol A, tetrabromobisphenol S and bovine trypsin by spectroscopies and molecular dynamics simulations

Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies

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