Articolo in rivista, 2018, ENG, 10.1166/jnn.2018.14333
Morozova EA, Kulikova VV, Faggiano S, Raboni S, Gabellieri E, Cioni P, Anufrieva NV, Revtovich SV, Demidkina T, Mozzarelli A
Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 119991, Russia Univ Parma, Dept Food & Drug, I-43124 Parma, Italy CNR, Inst Biophys, I-56124 Pisa, Italy
Methionine gamma-lyase is a pyridoxal 5'-phosphate dependent tetramer that catalyzes the alpha, gamma-elimination of methionine in ammonia, methanethiol and alpha-ketobutyrate. MGL catalytic power has been exploited as a therapeutic strategy to reduce the viability of cancer cells or bacteria. In order to obtain a stable enzyme to be delivered at the site of action, MGL can be encapsulated in a variety of matrices. As a reference encapsulation strategy we have prepared MGL nanoporous wet silica gels. Immobilized MGL gels were characterized with regards to activity, stability, absorption, circular dichroism and fluorescence properties and compared with soluble MGL. We found that MGL gels exhibit (i) spectroscopic properties very similar to MGL in solution, (ii) a higher stability with respect to the soluble enzyme and (iii) catalytic activity six-fold lower than in solution. These findings prove that MGL encapsulation is a suitable strategy for therapeutic applications.
Journal of nanoscience and nanotechnology (Print) 18 (3), pp. 2210–2219
Methionine; Protein Drug; Protein Encapsulation; Pyridoxal Phosphate; Enzyme Activity; Fluorescence
Mozzarelli Andrea, Raboni Samanta, Gabellieri Edi, Cioni Patrizia
ID: 387270
Year: 2018
Type: Articolo in rivista
Creation: 2018-05-15 13:11:15.000
Last update: 2021-04-08 17:11:36.000
CNR institutes
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:387270
DOI: 10.1166/jnn.2018.14333
ISI Web of Science (WOS): 000426033400124