title: Enzyme-triggered cargo release from methionine sulfoxide containing copolypeptide vesicles.
abstract: We have developed a facile, scalable method for preparation of enzyme-responsive copolypeptide vesicles that requires no protecting groups or expensive components. We designed amphiphilic copolypeptides containing segments of water-soluble methionine sulfoxide, M(O), residues that were prepared by synthesis of a fully hydrophobic precursor diblock copolypeptide, poly(l-methionine)65-b-poly(L-leucine0.5-stat-L-phenylalanine0.5)20, M65(L0.5/F0.5)20, followed by its direct oxidation in water to give the amphiphilic M(O) derivative, M(O)65(L0.5/F0.5)20. Assembly of M(O)65(L0.5/F0.5)20 in water gave vesicles with average diameters of a few micrometers that could then be extruded to nanoscale diameters. The M(O) segments in the vesicles were found to be substrates for reductase enzymes, which regenerated hydrophobic M segments and resulted in a change in supramolecular morphology that caused vesicle disruption and release of cargos.
authors: Department of Bioengineering and ‡Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
authors: April R
authors: AR
authors: Rodriguez
authors: Jessica R
authors: JR
authors: Kramer
authors: Timothy J
authors: TJ
authors: Deming
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008715:Methionine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D010088:Oxidoreductases / Q000378:metabolism*; D010316:Particle Size; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity; D013499:Surface Properties; D013501:Surface-Active Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism
chemical_list: D010455:Peptides; D013501:Surface-Active Agents; D008715:Methionine; D010088:Oxidoreductases; C013111:methionine sulfoxide