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Title: Membrane reconstitution of monoamine oxidase enzymes on supported lipid bilayers
Authors: Wang, Liulin
Kabir H. Biswas
Yoon, Bo Kyeong
Kawakami, Lisa M.
Park, Soohyun
Groves, Jay T.
Li, Lin
Huang, Wei
Cho, Nam-Joon
Keywords: Science::Medicine
Issue Date: 2018
Source: Wang, L., Kabir H. Biswas, Yoon, B. K., Kawakami, L. M., Park, S., Groves, J. T., . . . Cho, N.-J. (2018). Membrane reconstitution of monoamine oxidase enzymes on supported lipid bilayers. Langmuir, 34(36), 10764-10773. doi:10.1021/acs.langmuir.8b01348
Journal: Langmuir
Abstract: Monoamine oxidase A and B (MAO-A and B) are mitochondrial outer membrane enzymes that are implicated in a number of human diseases, and the pharmacological inhibition of these enzymes is a promising therapeutic strategy to alleviate disease symptoms. It has been suggested that optimal levels of enzymatic activity occur in the membrane-associated state, although details of the membrane association process remain to be understood. Herein, we have developed a supported lipid bilayer platform to study MAO-A and B binding and evaluate the effects of known pharmacological inhibitors on the membrane association process. By utilizing the quartz crystal microbalance-dissipation (QCM-D) technique, it was determined that both MAOs exhibit tight binding to negatively and positively charged bilayers with distinct concentration-dependent binding profiles while only transiently binding to neutral bilayers. Importantly, in the presence of known inhibitors, the MAOs showed increased binding to negatively charged bilayers, although there was no effect of inhibitor treatment on binding to positively charged bilayers. Taken together, our findings establish that the membrane association of MAOs is highly dependent on membrane surface charge, and we outline an experimental platform to support the in vitro reconstitution of monoamine oxidases on synthetic membranes, including the evaluation of pharmacological drug candidates.
ISSN: 0743-7463
DOI: 10.1021/acs.langmuir.8b01348
Rights: © 2018 American Chemical Society. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:MSE Journal Articles

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