Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength

Yamasaki, Miyuki; Yano, Hiroshige; Aoki, Koichiro

doi:10.1016/0141-8130(90)90007-w

Cited by 145 publications

(106 citation statements)

References 14 publications

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“…8d). The MRE 222 nm decreases with the rise in temperature, which may be due to a loss of higher order secondary structure, i.e., a-helix [38]. The midpoint temperature (T m ) was determined by fitting the ellipticity values into a two-state folding-unfolding model Eqs.…”

Section: Effect Of Ax On Thermal Stability Of Hsamentioning

confidence: 99%

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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Amoxicillin is a common antibiotic drug used for preventing bacterial colonization of urinary and skin infections. The binding of amoxicillin (AX) to human serum albumin (HSA) in sodium phosphate buffer solution at pH 7.4 has been investigated by UV-visible spectroscopy, fluorescence spectroscopy, Förster resonance energy transfer, isothermal titration calorimetry (ITC), circular dichroism (CD) and FTIR spectroscopy. The binding studies using ITC revealed that the interaction is entropy driven rather than enthalpy as the change in enthalpy (DH°) and change in entropy (TDS°) both are positive, indicating the endothermic reaction with low affinity and hydrophobic interaction. UV-visible absorption spectra of HSA are increased upon addition of AX which shows complex formation of HSA-AX. The fluorescence spectra reveal that the AX has an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The molecular distance r between donor (HSA) and acceptor (AX) was estimated according to Förster theory of nonradiative energy transfer. The CD spectra showed that the a-helix of HSA increases with increasing the amount of AX. The thermal denaturation has been studied by far-UV CD, and it is found that HSA stability is decreased by the complex formation of HSA and AX. The remarkable change in amide I peak position in infrared spectrum after interaction with AX indicated that secondary structure of HSA has been changed.

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Section: Effect Of Ax On Thermal Stability Of Hsamentioning

confidence: 99%

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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“…The representative DSC profiles of thermal denaturation of BSA in the absence and the presence of varying molalities of TFE at pH 7.0 are shown in Figure 1, and the corresponding thermodynamic parameters accompanying the thermal transitions are presented in Table I 35 With an increase in the TFE molality from 0.1 to 1.0 mol kg…”

Section: Dsc Of Bsa In the Presence Of Tfementioning

confidence: 99%

Does the anesthetic 2,2,2‐trifluoroethanol interact with bovine serum albumin by direct binding or by solvent‐mediated effects? A calorimetric and spectroscopic investigation

Banerjee

Kishore

2005

Biopolymers

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Thermal unfolding of bovine serum albumin (BSA) has been studied in the presence of 2,2,2-trifluoroethanol (TFE) using high-sensitivity microdifferential scanning calorimetry. Quantitative thermodynamic parameters accompanying the thermal transitions have been evaluated. TFE is observed to be a stabilizer or a destabilizer of the folded state of BSA depending on the pH. CD spectroscopy revealed an increase in the -helical content of BSA and a decrease in the tertiary structure in the presence of increasing molalities of TFE. Isothermal titration calorimetric results do not indicate appreciable binding of the TFE molecules to BSA. TFE quenches the steady-state tryptophan fluorescence of BSA only at higher molalities and there is no effect on the tryptophan fluorescence at lower molalities. The calorimetric and spectroscopic results obtained in this work suggest that solvent-mediated effects dominate the interaction of TFE with BSA and the binding component may be very weak. Since the binding component is very weak, one of the possibilities of anesthetic action of TFE molecules on the actual targets may be through perturbation of the structural and dynamic properties of the lipid bilayer so that the function of crucial but unspecified membrane proteins is affected. C 2005 Wiley Periodicals, Inc. Biopolymers 78: [78][79][80][81][82][83][84][85][86] 2005 This article was originally published online as an accepted preprint. The ''Published Online''date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…[4][5][6][7][8][9][10][11][12][13][14] The status of bovine serum albumin (BSA) during denaturation has been analyzed and confirmed using far-ultraviolet circular dichroisom. 13,14 Thermal analysis using differential scanning calorimetry (DSC) discloses the thermodynamic conditions under which denaturation occurs and quantifies the enthalpy of denaturation.…”

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confidence: 99%

“…[4][5][6][7][8]18 It has been reported that DSC studies of BSA reveal the thermodynamics of the protein associated with denaturation, specifically the change in specific heat and enthalpy near the denaturation temperature T d . [6][7][8] However, relatively less attention has been paid to k of BSA (k BSA ). 18 Therefore, we measured k of aqueous solutions of BSA (k sol ) by varying T and pH to determine how denaturation affects thermal transport in the solutions.…”

mentioning

confidence: 99%

“…18 Therefore, we measured k of aqueous solutions of BSA (k sol ) by varying T and pH to determine how denaturation affects thermal transport in the solutions. The measured k data were compared with the results of the DSC analysis, 7 with discussions on the correlation between k and the denaturation process. BSA solutions were prepared by mixing BSA powder (biotechnology grade BSA, 0903, AMRESCO) with deionized (DI) water.…”

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Thermal conductivity of bovine serum albumin: A tool to probe denaturation of protein

Park

et al. 2011

Applied Physics Letters

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We demonstrate a strong correlation between denaturation of bovine serum albumin (BSA) and the thermal conductivity k of aqueous solutions of BSA. When denaturation of BSA began, k dropped significantly. These results suggest that k, i.e., the ability of a protein to transport passively applied thermal energy, can be exploited to probe the conformational dynamics of BSA and potentially of other proteins. The technique of protein analysis demonstrated in this work is expected to be useful in micro-total-analysis systems because it is easier to miniaturize and to integrate into a device than is conventional differential scanning calorimetry analysis.

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Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength

Cited by 145 publications

References 14 publications

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Does the anesthetic 2,2,2‐trifluoroethanol interact with bovine serum albumin by direct binding or by solvent‐mediated effects? A calorimetric and spectroscopic investigation

Thermal conductivity of bovine serum albumin: A tool to probe denaturation of protein

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