TY - JOUR
T1 - Nanodiscs and mass spectrometry
T2 - Making membranes fly
AU - Marty, Michael T.
N1 - Funding Information:
Michael T. Marty, Ph.D., is an Assistant Professor in the Department of Chemistry & Biochemistry and Bio5 Institute at The University of Arizona. Prof. Marty earned his B.A. in chemistry and mathematics at St. Olaf College in 2010, and he completed his Ph.D. in chemistry as a Springborn Fellow at the University of Illinois Urbana-Champaign in 2013 under the direction of Prof. Stephen Sligar. He then performed postdoctoral research at the University of Oxford with Prof. Dame Carol Robinson before joining the faculty at The University of Arizona in 2016. Prof. Marty has been awarded the ASMS Research Award, the Bisgrove Scholar Award, an NSF CAREER award, and an NIH R35 Maximizing Investigators’ Research Award (MIRA). His research applies lipoprotein nanodiscs with mass spectrometry to study membrane proteins, antimicrobial peptides, and their interactions with lipid bilayers. As the developer of UniDec, he is also interested in mass spectrometry data analysis and deconvolution.
Funding Information:
The author thanks many friends, collaborators, and mentors for outstanding support, especially Carol Robinson, Stephen Sligar, and Michael Gross. Recent work was done by a talented team of high school students, undergraduates, graduates, and staff scientists, and the author thanks them all for making the lab such a fun and exciting place to work. Current research interfacing nanodiscs and native MS is funded by the National Science Foundation ( CHE-1845230 ) and the National Institute of General Medical Sciences and National Institutes of Health ( R35 GM128624 ). The content is solely the responsibility of the author and does not necessarily represent the official views of the NIH.
Publisher Copyright:
© 2020 Elsevier B.V.
PY - 2020/12
Y1 - 2020/12
N2 - Cells are surrounded by a protective lipid bilayer membrane, and membrane proteins in the bilayer control the flow of chemicals, information, and energy across this barrier. Many therapeutics target membrane proteins, and some directly target the lipid membrane itself. However, interactions within biological membranes are challenging to study due to their heterogeneity and insolubility. Mass spectrometry (MS) has become a powerful technique for studying membrane proteins, especially how membrane proteins interact with their surrounding lipid environment. Although detergent micelles are the most common membrane mimetic, nanodiscs are emerging as a promising platform for MS. Nanodiscs, nanoscale lipid bilayers encircled by two scaffold proteins, provide a controllable lipid bilayer for solubilizing membrane proteins. This Young Scientist Perspective focuses on native MS of intact nanodiscs and highlights the unique experiments enabled by making membranes fly, including studying membrane protein-lipid interactions and exploring the specificity of fragile transmembrane peptide complexes. It will also explore current challenges and future perspectives for interfacing nanodiscs with MS.
AB - Cells are surrounded by a protective lipid bilayer membrane, and membrane proteins in the bilayer control the flow of chemicals, information, and energy across this barrier. Many therapeutics target membrane proteins, and some directly target the lipid membrane itself. However, interactions within biological membranes are challenging to study due to their heterogeneity and insolubility. Mass spectrometry (MS) has become a powerful technique for studying membrane proteins, especially how membrane proteins interact with their surrounding lipid environment. Although detergent micelles are the most common membrane mimetic, nanodiscs are emerging as a promising platform for MS. Nanodiscs, nanoscale lipid bilayers encircled by two scaffold proteins, provide a controllable lipid bilayer for solubilizing membrane proteins. This Young Scientist Perspective focuses on native MS of intact nanodiscs and highlights the unique experiments enabled by making membranes fly, including studying membrane protein-lipid interactions and exploring the specificity of fragile transmembrane peptide complexes. It will also explore current challenges and future perspectives for interfacing nanodiscs with MS.
KW - Antimicrobial peptides
KW - Lipids
KW - Membrane proteins
KW - Nanodiscs
KW - Native mass spectrometry
KW - Protein-lipid interactions
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U2 - 10.1016/j.ijms.2020.116436
DO - 10.1016/j.ijms.2020.116436
M3 - Article
AN - SCOPUS:85091659346
VL - 458
JO - International Journal of Mass Spectrometry and Ion Processes
JF - International Journal of Mass Spectrometry and Ion Processes
SN - 1387-3806
M1 - 116436
ER -