Several lipase enzymes catalyze the degradation of micelles derived from poly (e-caprolactone) (PCL) block poly (ethylene glycol) (PEG) diblock copolymers (HO-PCL-b-PEG-OMe) through PCL ester hydrolysis. Spherical micelles with charged corona exteriors derived from block copolymers with charged PEG end groups (HO-PCLn-b-PEG32-RX, R=-O(CH2)3S(CH2)2-; X= -CO2-, -SO3-, -NH3+) were designed and prepared to probe the corona charge effects on enzyme catalysis. The working hypothesis was that when the micelle corona and lipase enzymes have the same charge there will be an increased barrier to reaction which could be used as a design feature to obtain selectivity for therapeutic transport and release. Kinetic studies of P.cepacia lipase catalyzed degradation of micelles with charged corona will be described and discussed that illustrate fulfillment of this hypothesis. Two closely related P.cepacia lipase isoforms are observed to manifest unprecedented complementary micelle corona charge selective catalysis.

Charge selective lipase enzyme-block copolymer micelle binding, interfacial activation and catalytic degradation

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.