Effects of polymer molecular weight on the size, activity, and stability of PEG-functionalized trypsin.

Abstract:

:Polymer conjugation increases an enzyme's circulation time and stability for use as a therapeutic agent, but this attachment indubitably affects its properties. Covalent attachment of multiple polyethylene glycol chains with sizes of either 2, 5, 10, or 20 kDa increases the molecular weight and hydrodynamic radius of the model enzyme trypsin. The sizes of these polymer-enzyme conjugates are increased to be within the recommended limits for PDEPT applications. The T(d) increases from 49 to 60 °C to expand the enzyme's workable range of conditions. This functionalization with PEG polymers of varying lengths maintains trypsin's enzymatic activity. Conjugate activities are 79-120% that of native trypsin at room temperature and 221-432% that of trypsin at 37 °C.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Chiu K,Agoubi LL,Lee I,Limpar MT,Lowe JW Jr,Goh SL

doi

10.1021/bm1006954

subject

Has Abstract

pub_date

2010-12-13 00:00:00

pages

3688-92

issue

12

eissn

1525-7797

issn

1526-4602

journal_volume

11

pub_type

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