TY - JOUR
T1 - Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates: A calorimetric study
AU - Pelosi, C.
AU - Saitta, F.
AU - Wurm, F.R.
AU - Fessas, D.
AU - Tinè, M.R.
AU - Duce, C.
PY - 2019/1/1
Y1 - 2019/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-85056583374&partnerID=MN8TOARS
U2 - 10.1016/j.tca.2018.11.001
DO - 10.1016/j.tca.2018.11.001
M3 - Article
SN - 0040-6031
VL - 671
SP - 26
EP - 31
JO - Thermochimica acta
JF - Thermochimica acta
ER -