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
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Chiu K,Agoubi LL,Lee I,Limpar MT,Lowe JW Jr,Goh SLdoi
10.1021/bm1006954subject
Has Abstractpub_date
2010-12-13 00:00:00pages
3688-92issue
12eissn
1525-7797issn
1526-4602journal_volume
11pub_type
杂志文章abstract::We report the rational design of a chitosan-based drug delivery system. The chitosan derivative N-[(2-hydroxy-3-trimethylammonium)propyl]chitosan chloride (HTCC) was ionically cross-linked by sodium tripolyphosphate (TPP) to form sub-200-nm microgels that are responsive to pH changes. When these microgels were loaded ...
journal_title:Biomacromolecules
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