PMID: 11312676Apr 21, 2001Paper

Drug delivery systems employing 1,6-elimination: releasable poly(ethylene glycol) conjugates of proteins

Bioconjugate Chemistry
S LeeC Shi

Abstract

Using lysozyme as a representative protein substrate that loses its activity when PEGylation takes place on the epsilon-amino group of lysine residues, various amounts of a novel releasable PEG linker (rPEG) were conjugated to the protein. rPEG-lysozyme conjugates were relatively stable in pH 7.4 buffer for over 24 h. However, regeneration of native protein from the rPEG conjugates occurred in a predictable manner during incubation in high pH buffer or rat plasma, as demonstrated by enzymatic activity and structural characterization. The rates of regeneration were also correlated with PEG number: native lysozyme was released more rapidly from the monosubstituted conjugate than from the disubstituted conjugate, suggesting possible steric hindrance to the approach of cleaving enzymes. Recovery of normal activity and structure for the regenerated native lysozyme was shown by a variety of assays.

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Citations

Feb 5, 2010·Biotechnology Letters·A ConstantinouM P Deonarain
Jun 25, 2013·Pharmaceutical Research·Muhammad Sajid Hamid AkashShuqing Chen
Aug 8, 2001·Journal of Controlled Release : Official Journal of the Controlled Release Society·R B Greenwald
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Dec 1, 2016·Nature Reviews. Materials·Jianyu Li, David J Mooney
Jul 22, 2010·Pharmaceutical Biology·Débora da Silva Freitas, José Abrahão-Neto
Feb 26, 2021·Macromolecular Rapid Communications·Maximilian SchergerLutz Nuhn
Jan 26, 2010·Biomacromolecules·Ferdinand BrandlAchim Goepferich
Mar 18, 2021·Annual Review of Chemical and Biomolecular Engineering·Souvik GhosalChristopher A Alabi
Jan 13, 2011·Bioconjugate Chemistry·Aram O SaeedCameron Alexander
Mar 24, 2010·International Journal of Pharmaceutics·Débora da Silva Freitas, José Abrahão-Neto
Nov 4, 2021·Bioconjugate Chemistry·Thaiesha A WrightDominik Konkolewicz

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