Journal of Undergraduate Research
Keywords
PEGylation, thermodynamic stability, WW domain, Pin1, hydrogen bonding
College
Physical and Mathematical Sciences
Department
Chemistry and Biochemistry
Abstract
Proteins are complex molecules that have the potential to treat diseases and illnesses that small molecule drugs cannot. However, a significant problem with protein medications is that proteins tend to have short serum half-lives and can be difficult to store for extended periods of time due to their often unstable nature.1 One widely used strategy to circumvent these problems and increase the serum half-life of protein drugs is to attach polyethylene glycol (PEG) oligomers to amino acid residues (i.e., PEGylation) of protein structures.2 The thermodynamic effects of PEGylation are not always positive, however, and currently difficult to predict.3 In order to better comprehend and predict the effects PEGylation will have on protein stability, we must determine how PEG interacts with the protein and understand the nature of that interaction.
Recommended Citation
Torgerson, Chad and Price, Dr. Joshua
(2013)
"Does PEGylation Increase the Thermodynamic Stability of the WW domain of Pin1 via Hydrogen Bonding? A Molecular Dynamics Simulation,"
Journal of Undergraduate Research: Vol. 2013:
Iss.
1, Article 2574.
Available at:
https://scholarsarchive.byu.edu/jur/vol2013/iss1/2574