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.
|Titolo:||Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates : a calorimetric study|
SAITTA, FRANCESCA (Co-primo)
FESSAS, DIMITRIOS (Corresponding)
|Parole Chiave:||Calorimetry; PEGylation; Protein unfolding; Protein-polymer conjugation; Unfolding reversibility; Instrumentation; Condensed Matter Physics; Physical and Theoretical Chemistry|
|Settore Scientifico Disciplinare:||Settore CHIM/02 - Chimica Fisica|
|Data di pubblicazione:||gen-2019|
|Data ahead of print / Data di stampa:||5-nov-2018|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1016/j.tca.2018.11.001|
|Appare nelle tipologie:||01 - Articolo su periodico|