Exploration of interactions between membrane proteins embedded in supported lipid bilayers and their antibodies by reflectometric interference spectroscopy-based sensing

The Analyst ◽  
2014 ◽  
Vol 139 (22) ◽  
pp. 6016-6021 ◽  
Author(s):  
Yoshikazu Kurihara ◽  
Tsuneo Sawazumi ◽  
Toshifumi Takeuchi
Keyword(s):  
Multidrug Resistance ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Model Membrane ◽  
Supported Lipid Bilayers ◽  
Reflectometric Interference Spectroscopy

A microfluidic reflectometric interference spectroscopy (RIfS)-based sensor was fabricated to investigate the activity of multidrug resistance-associated protein 1 (MRP1), applied as a model membrane protein.

Mutations in transmembrane proteins: diseases, evolutionary insights, prediction and comparison with globular proteins

2020 ◽  
Author(s):  
Jan Zaucha ◽  
Michael Heinzinger ◽  
A Kulandaisamy ◽  
Evans Kataka ◽  
Óscar Llorian Salvádor ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Protein Structures ◽  
Experimental Studies ◽  
Single Amino Acid ◽  
Evolutionary Information ◽  
Missense Variants ◽  
Current State ◽  
Aqueous Environments

Abstract Membrane proteins are unique in that they interact with lipid bilayers, making them indispensable for transporting molecules and relaying signals between and across cells. Due to the significance of the protein’s functions, mutations often have profound effects on the fitness of the host. This is apparent both from experimental studies, which implicated numerous missense variants in diseases, as well as from evolutionary signals that allow elucidating the physicochemical constraints that intermembrane and aqueous environments bring. In this review, we report on the current state of knowledge acquired on missense variants (referred to as to single amino acid variants) affecting membrane proteins as well as the insights that can be extrapolated from data already available. This includes an overview of the annotations for membrane protein variants that have been collated within databases dedicated to the topic, bioinformatics approaches that leverage evolutionary information in order to shed light on previously uncharacterized membrane protein structures or interaction interfaces, tools for predicting the effects of mutations tailored specifically towards the characteristics of membrane proteins as well as two clinically relevant case studies explaining the implications of mutated membrane proteins in cancer and cardiomyopathy.

Peptide Disc Mediated Control of Membrane Protein Orientation in Supported Lipid Bilayers for Surface-Sensitive Investigations

2019 ◽  
Vol 92 (1) ◽  
pp. 1081-1088 ◽  
Author(s):  
Alessandra Luchini ◽  
Frederik Grønbæk Tidemand ◽  
Nicolai Tidemand Johansen ◽  
Mario Campana ◽  
Javier Sotres ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Supported Lipid Bilayers ◽  
Protein Orientation

scholarly journals Evidence for Membrane Complex Assembly in Nanoelectrospray Generated Lipid Bilayers

2019 ◽  
Author(s):  
Matthias Wilm
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Layered Structure ◽  
Protein Complexes ◽  
Complex Assembly ◽  
Membrane Complex ◽  
Detergent Extraction ◽  
Membrane Protein Complexes

1.AbstractNanoelectrospray can be used to generate a layered structure consisting of bipolar lipids, detergent-solubilized membrane proteins, and glycerol that self-assembles upon detergent extraction into one extended layer of a protein containing membrane. This manuscript presents the first evidence that this method might allow membrane protein complexes to assemble in this process.

scholarly journals Assembly of Model Membrane Nanodiscs for Native Mass Spectrometry

2021 ◽  
Author(s):  
Marius Kostelic ◽  
Ciara K. Zak ◽  
Hiruni Jayasekera ◽  
Michael Marty
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Biological Membranes ◽  
Native Mass Spectrometry ◽  
Model Membrane ◽  
Peptide Interactions ◽  
Lipid Nanodiscs ◽  
Natural Lipid ◽  
Selection Of

Native mass spectrometry (MS) with nanodiscs is a promising technique for characterizing membrane protein and peptide interactions in lipid bilayers. However, prior studies have used nanodiscs made of only one or two lipids, which lack the complexity of a natural lipid bilayer. To better model specific biological membranes, we developed model mammalian, bacterial, and mitochondrial nanodiscs with up to four different phospholipids. Careful selection of lipids with similar masses that balance the fluidity and curvature enabled these complex nanodiscs to be assembled and resolved with native MS. We then applied this approach to characterize the specificity and incorporation of LL-37, a human antimicrobial peptide, in single lipid nanodiscs versus model bacterial nanodiscs. Overall, development of these model membrane nanodiscs reveals new insights into the assembly of complex nanodiscs and provides a useful toolkit for studying membrane protein, peptide, and lipid interactions in model biological membranes.

scholarly journals Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins

Crystals ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 1032
Author(s):  
Sonia Khemaissa ◽  
Sandrine Sagan ◽  
Astrid Walrant
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Hydrogen Bonds ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Noncovalent Interactions ◽  
Chemical Properties ◽  
Protein Stabilization ◽  
Physico Chemical

Tryptophan is an aromatic amino acid with unique physico-chemical properties. It is often encountered in membrane proteins, especially at the level of the water/bilayer interface. It plays a role in membrane protein stabilization, anchoring and orientation in lipid bilayers. It has a hydrophobic character but can also engage in many types of interactions, such as π–cation or hydrogen bonds. In this review, we give an overview of the role of tryptophan in membrane proteins and a more detailed description of the underlying noncovalent interactions it can engage in with membrane partners.

scholarly journals Controlling transmembrane protein concentration and orientation in supported lipid bilayers

2017 ◽  
Vol 53 (30) ◽  
pp. 4250-4253 ◽  
Author(s):  
P. Bao ◽  
M. L. Cartron ◽  
K. H. Sheikh ◽  
B. R. G. Johnson ◽  
C. N. Hunter ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayers ◽  
Electric Fields ◽  
Protein Concentration ◽  
Transmembrane Protein ◽  
Fold Increase ◽  
Supported Lipid Bilayers

The trans-membrane protein–proteorhodopsin (pR) has been incorporated into supported lipid bilayers (SLB). In-plane electric fields have been used to manipulate the orientation and concentration of these proteins, within the SLB, through electrophoresis leading to a 25-fold increase concentration of pR.

Electrophoretic mobility of a monotopic membrane protein inserted into the top of supported lipid bilayers

2016 ◽  
Vol 39 (12) ◽  
Author(s):  
Frédéric Harb ◽  
Marie-Thérèse Giudici-Orticoni ◽  
Marianne Guiral ◽  
Bernard Tinland
Keyword(s):  
Membrane Protein ◽  
Electrophoretic Mobility ◽  
Lipid Bilayers ◽  
Supported Lipid Bilayers
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