Effect of polyethylene glycol on the thermal stability of green fluorescent protein.
Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. Some polymers, such as polyethylene glycol, are often used as modifiers of characteristics of biological macromolecules, to improve the biochemical activity and stability of proteins or drug bioavailability. The aim of this study was to evaluate the thermal stability of GFP in the presence of different PEG molar weights at several concentrations and exposed to constant temperatures, in a range of 70-95 degrees C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were almost constant for temperatures of 85, 90, and 95 degrees C, despite the PEG concentration or molar weight studied. Even though PEG can stabilize proteins, only at 75 degrees C, PEG 600 and 4,000 g/mol stabilized GFP.
Dept. of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, SP, Brazil. lclnovaes@usp.br
Letícia C
LC
de Lencastre Novaes
Priscila G
PG
Mazzola
Adalberto
A
Pessoa
Thereza C Vessoni
TC
Penna
D049452:Green Fluorescent Proteins / Q000737:chemistry*; D008970:Molecular Weight; D011092:Polyethylene Glycols / Q000737:chemistry*; D055550:Protein Stability; D013696:Temperature
D049452:Green Fluorescent Proteins; D011092:Polyethylene Glycols