Assessment of interactions between four proteins and benzothiazole derivatives by DSC and CD

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• 作者：Natalia Hassan^a ; Pedro V. Verdes ; ^a ; ^{pedro.vazquez@usc.es} ; Juan M. Ruso^a
• 关键词：3-(2-Benzothiazolylthio)-1-propanesulfonic acid (BTS) ; Protein ; Differential scanning calorimetry ; Thermal denaturation ; Circular dichroism
• 刊名：Journal of Chemical Thermodynamics
• 出版年：2011
• 出版时间：March 2011
• 年：2011
• 卷：43
• 期：3
• 页码：399-404
• 全文大小：705 K

文摘

The thermal denaturation of ovalbumin, lysozyme, myoglobin and fibrinogen at different BTS concentrations have been investigated using differential scanning calorimetry (DSC) and circular dichroism (CD) spectroscopy. Thermodynamic parameters: melting temperatures (T_m), calorimetric enthalpy (ΔH), van’t Hoff enthalpy (ΔH_v) were obtained for all the systems under study. Thermal denaturation of the four proteins was completely irreversible. Changes in the protein conformation due to the adsorption of BTS molecules have been monitored by using UV-CD spectra. Greater changes in α-helical contents correspond with the BTS higher concentrations. The lysozyme denaturation temperature increases at low concentrations BTS indicating that BTS acts as a structure stabilizer; meanwhile it acts as a destabilizer at higher concentrations in all the proteins studied. The major effect is observed in the case of myoglobin, the protein with the highest α-helical secondary structure (75 % ).