PEGylated proteins are widely used for therapeutic applications, therefore a fundamental understanding of the conjugates’ structure and their behaviour in solution is essential to promote new developments in this field. In the present work, myoglobin-poly(ethylene glycol) conjugates were synthesized and studied by differential scanning calorimetry and UV–vis spectroscopy to obtain information on the bioconjugates’ thermodynamic stability, also focusing on PEG's role on the solvent-protein surface interaction. The overall results of this study indicated a thermal destabilization of the protein that follows the extent of the bioconjugation without, however, compromising the native structure which remains functional. Moreover, the myoglobin PEGylation prevented the post-denaturation aggregation phenomena and enhanced the protein thermal reversibility. The thermodynamic interpretation of the data indicated that the bioconjugation influences the solvent-exposed protein surface difference between native and denatured state, contributing to the interpretation of the overall protein modification and functionality.
Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates : a calorimetric study / C. Pelosi, F. Saitta, F.R. Wurm, D. Fessas, M.R. Tinè, C. Duce. - In: THERMOCHIMICA ACTA. - ISSN 0040-6031. - 671(2019 Jan), pp. 26-31. [10.1016/j.tca.2018.11.001]
Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates : a calorimetric study
F. SaittaCo-primo
;D. Fessas
;
2019
Abstract
PEGylated proteins are widely used for therapeutic applications, therefore a fundamental understanding of the conjugates’ structure and their behaviour in solution is essential to promote new developments in this field. In the present work, myoglobin-poly(ethylene glycol) conjugates were synthesized and studied by differential scanning calorimetry and UV–vis spectroscopy to obtain information on the bioconjugates’ thermodynamic stability, also focusing on PEG's role on the solvent-protein surface interaction. The overall results of this study indicated a thermal destabilization of the protein that follows the extent of the bioconjugation without, however, compromising the native structure which remains functional. Moreover, the myoglobin PEGylation prevented the post-denaturation aggregation phenomena and enhanced the protein thermal reversibility. The thermodynamic interpretation of the data indicated that the bioconjugation influences the solvent-exposed protein surface difference between native and denatured state, contributing to the interpretation of the overall protein modification and functionality.File | Dimensione | Formato | |
---|---|---|---|
Myoglobin ThermActa2018-19.pdf
accesso riservato
Tipologia:
Publisher's version/PDF
Dimensione
2.54 MB
Formato
Adobe PDF
|
2.54 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.