Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins

Integral membrane proteins (IMPs) fulfill important physiological functions by providing cell–environment, cell–cell and virus–host communication; nutrients intake; export of toxic compounds out of cells; and more. However, some IMPs have obliterated functions due to polypeptide mutations, modificat...

Full description

Bibliographic Details
Main Authors: Saman Majeed, Akram Bani Ahmad, Ujala Sehar, Elka R. Georgieva
Format: Article
Language:English
Published: MDPI AG 2021-09-01
Series:Membranes
Subjects:
Online Access:https://www.mdpi.com/2077-0375/11/9/685
_version_ 1797518193924767744
author Saman Majeed
Akram Bani Ahmad
Ujala Sehar
Elka R. Georgieva
author_facet Saman Majeed
Akram Bani Ahmad
Ujala Sehar
Elka R. Georgieva
author_sort Saman Majeed
collection DOAJ
description Integral membrane proteins (IMPs) fulfill important physiological functions by providing cell–environment, cell–cell and virus–host communication; nutrients intake; export of toxic compounds out of cells; and more. However, some IMPs have obliterated functions due to polypeptide mutations, modifications in membrane properties and/or other environmental factors—resulting in damaged binding to ligands and the adoption of non-physiological conformations that prevent the protein from returning to its physiological state. Thus, elucidating IMPs’ mechanisms of function and malfunction at the molecular level is important for enhancing our understanding of cell and organism physiology. This understanding also helps pharmaceutical developments for restoring or inhibiting protein activity. To this end, in vitro studies provide invaluable information about IMPs’ structure and the relation between structural dynamics and function. Typically, these studies are conducted on transferred from native membranes to membrane-mimicking nano-platforms (membrane mimetics) purified IMPs. Here, we review the most widely used membrane mimetics in structural and functional studies of IMPs. These membrane mimetics are detergents, liposomes, bicelles, nanodiscs/Lipodisqs, amphipols, and lipidic cubic phases. We also discuss the protocols for IMPs reconstitution in membrane mimetics as well as the applicability of these membrane mimetic-IMP complexes in studies via a variety of biochemical, biophysical, and structural biology techniques.
first_indexed 2024-03-10T07:26:44Z
format Article
id doaj.art-178f6268e79d4356876df06a28141fe4
institution Directory Open Access Journal
issn 2077-0375
language English
last_indexed 2024-03-10T07:26:44Z
publishDate 2021-09-01
publisher MDPI AG
record_format Article
series Membranes
spelling doaj.art-178f6268e79d4356876df06a28141fe42023-11-22T14:10:23ZengMDPI AGMembranes2077-03752021-09-0111968510.3390/membranes11090685Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane ProteinsSaman Majeed0Akram Bani Ahmad1Ujala Sehar2Elka R. Georgieva3Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USADepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USADepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USADepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USAIntegral membrane proteins (IMPs) fulfill important physiological functions by providing cell–environment, cell–cell and virus–host communication; nutrients intake; export of toxic compounds out of cells; and more. However, some IMPs have obliterated functions due to polypeptide mutations, modifications in membrane properties and/or other environmental factors—resulting in damaged binding to ligands and the adoption of non-physiological conformations that prevent the protein from returning to its physiological state. Thus, elucidating IMPs’ mechanisms of function and malfunction at the molecular level is important for enhancing our understanding of cell and organism physiology. This understanding also helps pharmaceutical developments for restoring or inhibiting protein activity. To this end, in vitro studies provide invaluable information about IMPs’ structure and the relation between structural dynamics and function. Typically, these studies are conducted on transferred from native membranes to membrane-mimicking nano-platforms (membrane mimetics) purified IMPs. Here, we review the most widely used membrane mimetics in structural and functional studies of IMPs. These membrane mimetics are detergents, liposomes, bicelles, nanodiscs/Lipodisqs, amphipols, and lipidic cubic phases. We also discuss the protocols for IMPs reconstitution in membrane mimetics as well as the applicability of these membrane mimetic-IMP complexes in studies via a variety of biochemical, biophysical, and structural biology techniques.https://www.mdpi.com/2077-0375/11/9/685integral membrane proteinslipid membrane mimeticsdetergent micellesbicellesnanodiscsliposomes
spellingShingle Saman Majeed
Akram Bani Ahmad
Ujala Sehar
Elka R. Georgieva
Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
Membranes
integral membrane proteins
lipid membrane mimetics
detergent micelles
bicelles
nanodiscs
liposomes
title Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
title_full Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
title_fullStr Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
title_full_unstemmed Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
title_short Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
title_sort lipid membrane mimetics in functional and structural studies of integral membrane proteins
topic integral membrane proteins
lipid membrane mimetics
detergent micelles
bicelles
nanodiscs
liposomes
url https://www.mdpi.com/2077-0375/11/9/685
work_keys_str_mv AT samanmajeed lipidmembranemimeticsinfunctionalandstructuralstudiesofintegralmembraneproteins
AT akrambaniahmad lipidmembranemimeticsinfunctionalandstructuralstudiesofintegralmembraneproteins
AT ujalasehar lipidmembranemimeticsinfunctionalandstructuralstudiesofintegralmembraneproteins
AT elkargeorgieva lipidmembranemimeticsinfunctionalandstructuralstudiesofintegralmembraneproteins