Now showing items 1-2 of 2
Site-specific PEGylation of native disulfide bonds in therapeutic proteins
Native disulfide bonds in therapeutic proteins are crucial for tertiary structure and biological activity and are therefore considered unsuitable for chemical modification. We show that native disulfides in human interferon ...
PEGylation of native disulfide bonds in proteins
PEGylation has turned proteins into important new biopharmaceuticals. The fundamental problems with the existing approaches to PEGylation are inefficient conjugation and the formation of heterogeneous mixtures. This is ...