The Surface of Protein λ_6-85 Can Act as a Template for Recurring Poly(ethylene glycol) Structure.

ABSTRACT: PEGylated proteins play an increasingly important role in pharmaceutical drug delivery. We recently showed that short poly(ethylene glycol) (PEG) chains can affect protein structure, even when they are not making extensive contact with the protein surface. In contrast, PEG is generally thought to form a relatively unstructured coil, and its compactness depends on solvent conditions. Here we test whether a host protein could allow PEG to form recurrent structural motifs while the PEG chain is in contact with the protein surface. We link a PEG oligomer (n = 45) to one of two nearly opposite locations on the small α-helical protein λ_6-85 to investigate this question. We first demonstrate experimentally that in these particular positions, PEG does not significantly affect the thermo

SUBMITTER: Chao SH 

PROVIDER: S-EPMC6044911 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature