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Investigation Into the Effects of PEGylation on the Thermodynamic Stability of the WW Domain

Sam Scrowcroft Matthews

出版	Brigham Young University. Department of Chemistry and Biochemistry, 2013
URL	http://books.google.com.hk/books?id=RGyxoQEACAAJ&hl=&source=gbs_api

註釋

This thesis details the results of two studies aimed at discovering the structural determinants which influence the thermodynamic impact of PEGylation on the WW domain, a small model protein. Chapter 1 is a brief introduction to protein therapeutics and protein PEGylation. Chapter 2 describes a study which demonstrates that the thermodynamic impact of PEGylation is strongly dependent on the site to which PEG is conjugated. The studies described in Chapter 3 elaborate on this site dependence, and demonstrate that PEG stabilizes the WW domain through interactions with the surface of the folded peptide, and that two factors-- the orientation of the PEG chain (relative to the protein surface) and the identity of nearby side chains-- play a critical role in determining the thermodynamic impact of PEGylation.