Applications of scanning microcalorimetry in biophysics and biochemistry

Shnyrov, Valery L.; Sánchez‐Ruiz, José M.; Бойко, Б. Н.; Zhadan, Galina G.; Permyakov, Eugene A.

doi:10.1016/s0040-6031(97)00238-4

Cited by 40 publications

(41 citation statements)

References 85 publications

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“…This includes the identification of a suitable FTIR data interpretation method that fits the T m (nDSC) values best and is applicable reliably over a wide range of differentially composed proteins, especially for measurements at higher protein concentrations (Q100 mg/mL). Because the nDSC technique requires low protein concentrations to avoid precipitation, thus preventing mechanical damaging of the sample cells (45,46), highly concentrated protein solutions have to be diluted before measurement. Therefore, the influence of protein concentration on T m (nDSC) could only be evaluated in the concentration range from 0.5 up to 5 mg/mL applicable for nDSC/mDSC.…”

Section: Determination Of T M (Ndsc) Of the Four Proteinsmentioning

confidence: 99%

“…Analytical methods applied in the designing and manufacturing of high-concentration protein formulations should avoid dilution of the protein solutions to measure the actual conditions and to prevent artifacts such as by potentially disturbing the protein's physical state (6). The concentration used in mDSC/nDSC analytics ranged from about 0.4 to 5 mg/mL to ensure that the effect of interactions between proteins is negligible and to avoid damage of the sample cells arising from the occurrence of precipitates favored at higher protein concentrations (45,46). This limitation is a major drawback of the method.…”

Section: Introductionmentioning

confidence: 99%

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FTIR and nDSC as Analytical Tools for High-Concentration Protein Formulations

2006

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Determination of a T(m (FTIR)) is feasible by the midpoint of the intensity-temperature plot of the arising intermolecular beta-sheet band. More significant results are obtained for proteins, which are predominantly composed of intramolecular beta-sheet elements as well as at higher protein concentrations. A further study was started to assess the predictability of long-term protein stability by T(m (FTIR)).

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Section: Determination Of T M (Ndsc) Of the Four Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

FTIR and nDSC as Analytical Tools for High-Concentration Protein Formulations

2006

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“…Furthermore, papers dealing with biochemical, biophysical and biological application of DSC should also be mentioned (Sturtevant 1987;Shnyrov et al 1997;Collett and Brown 1998;Levitzky et al 1998;Lorinczy 2004). Special attention has been devoted to the component of foods that infl uences decisively their functional properties -the proteins (Privalov 1989;Brandts and Lin 1990;Stanley and Yada 1992;Smith 1994;Freire 1995;Carey and Surewicz 1996;Boye et al 1997;Cooper 1999).…”

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confidence: 99%

Differential Scanning Calorimetry

Schubring

2009

Fishery Products

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Differential scanning calorimetry (DSC) is a well-established measuring method that is used on a large scale in different areas of research, development, and quality inspection and testing. Thermal effects can be quickly identifi ed and the relevant temperature and the characteristic caloric values determined using substance quantities in the mgmilligram range. Measurement values obtained by DSC allow heat capacity, heat of transition kinetic data, purity and glass transition to be determined. DSC curves serve to identify substances (Höhne et al. 1996). When a material undergoes a change in physical state such as melting or transition from one crystalline form to another, or when a material reacts chemically, heat is either absorbed or liberated. According to Lund (1983), DSC offers a tremendous potential for studying physicochemical changes that occur in foods. During the 1980s, its use in food research became apparent.DSC is characterised by its usefulness for analysing phase changes. Reactions that can lead to such phase changes are crystallisation of water (melting and freezing), evaporation of water and certain chemical reactions, for example protein denaturation. In DSC the temperature of the sample and reference are maintained the same and amount of heat required to achieve this is recorded. The DSC curve is a plot of heat fl ow against temperature. Consequently, the enthalpy change involved in the reaction can be determined from the area under the curve of heat-fl ow versus time. Material of known enthalpy can be used to calibrate the equipment. For samples containing water, evaporation is prevented using sealed containers. For examining frozen water in foods, results that are more reproducible are obtained while thawing frozen products than during cooling and freezing of products, because the variable phenomenon of super-cooling occurs during freezing. For proteins, the temperature corresponding to the maximum peak height is often used as an indication of the denaturation temperature, and the width of the peak as a measure of the complexity of the denaturation reaction. Using these assumptions, it is possible to observe how the denaturation temperature is affected by the changes in pH or the presence of other components, and the variation in enthalpy with denaturation temperature. As a protein becomes more denatured, the size of the peak should decrease. Phase changes in these both main components of the fi sh fl esh (water and protein) are subject of DSC investigation in this special fi eld. DSC has emerged 173 Fishery Products: Quality, safety and authenticity Edited by Hartmut Rehbein and Jörg Oehlenschläger

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“…DSC plays a remarkable role in studies involving biomolecule stabilization [12]. According to DSC analysis, change of the characteristic temperatures of the endothermic events were noted for both complexes, and a disappearance of some endothermic peaks was observed.…”

Section: Discussionmentioning

confidence: 99%

“…It defines the interactions of several molecules with proteins and their effects on the stability [12].…”

Section: Introductionmentioning

confidence: 99%

Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

et al. 2007

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Papain is a proteolytic enzyme with restricted applications due to its limited stability. Cyclodextrins are widely used in pharmaceutical formulations once they are able to form complexes with other molecules, improving their stability and bioavailability. The purpose of the present paper was to analyze complexes formed by papain/hydroxypropyl-β-cyclodextrin and papain/β-cyclodextrin by thermal analysis and cytotoxicity tests to verify their possible interactions and toxicological behavior. Complex solutions were prepared at different molar ratios and collected as a function of time to be lyophilized and analyzed. Results showed changes in endothermic events and cytotoxicity profiles. A complex formation for both complexes is observed; nevertheless, β-cyclodextrin was able to change the enzyme characteristics more efficiently.

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Applications of scanning microcalorimetry in biophysics and biochemistry

Cited by 40 publications

References 85 publications

FTIR and nDSC as Analytical Tools for High-Concentration Protein Formulations

FTIR and nDSC as Analytical Tools for High-Concentration Protein Formulations

Differential Scanning Calorimetry

Thermal Characterization and Cytotoxicity of Complexes Formed by Papain and Cyclodextrin

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