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Therapeutic nanoreactors: combining chemistry and biology in a novel triblock copolymer drug delivery system
Publication Type:
Journal ArticleSource:
Nanoletters, Volume 5, Issue 11, p.2220 - 2224 (2005)URL:
PM:16277457Keywords:
administration & dosage; Animals; Bacterial Outer Membrane Proteins; Bioreactors; Biotechnology; chemistry; Drug Delivery Systems; enzymology; Escherichia coli; Escherichia coli Proteins; ESCHERICHIA-COLI; Kinetics; Membrane Proteins; metabolism; N-GlycosAbstract:
Triblock copolymeric nanoreactors are introduced as an alternative for liposomes as encapsulating carrier for prodrug activating enzymes. Inosine-adenosine-guanosine preferring nucleoside hydrolase of Trypanosoma vivax, a potential prodrug activating enzyme, was encapsulated in nanometer-sized vesicles constructed of poly(2-methyloxazoline)-block-poly(dimethylsiloxane)-block-(2-methyloxazol ine) triblock copolymers. The nanoreactor is functionalized by incorporation of bacterial porins, OmpF or Tsx, in the reactor wall. Efficient cleavage of three natural substrates and one prodrug, 2-fluoroadenosine, by the nanoreactors was demonstrated
Notes:
DA - 20051109
IS - 1530-6984 (Print)
LA - eng
PT - In Vitro
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Outer Membrane Proteins)
RN - 0 (Escherichia coli Proteins)
RN - 0 (OmpF protein)
RN - 0 (Polymers)
RN - 0 (Porins)
RN - 0 (Prodrugs)
RN - 0 (Receptors, Virus)
RN - 134116-81-7 (Tsx protein, E coli)
RN - EC 3.2.2.- (N-Glycosyl Hydrolases)
RN - EC 3.2.2.- (inosine-adenosine-guanosine-preferring nucleoside hydrolase)
SB - IM