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Membrane Protein Based Biosensors
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Membrane Protein Based Biosensors

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 July 2015) | Viewed by 28919

Special Issue Editor

Dr. Bernhard Schuster

E-Mail Website
Guest Editor
Institute of Synthetic Bioarchitectures, Department of Bionanosciences, University of Natural Resources and Life Sciences, Muthgasse 11, 1190 Vienna, Austria
Interests: surface (S-)-layer proteins; biomimetics; self-assembly; functional supported lipid membranes; cell envelope structures of archaea; bioinspired materials; membrane-protein-based biosensors; bionanotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is dedicated to past and future developments in the field of biosensors whose receptive elements comprise either of (modified) membrane-active peptides, or of native or genetically engineered membrane-associated, as well as (trans)membrane proteins. The design of smart lipid membrane platforms is crucial for the functioning of membrane-active peptides and proteins, and can either be implemented by liposomal architectures, free-standing lipid bilayers, or planar lipid membranes attached to porous or solid supports. The single-molecule selectivity and specificity of the binding process, together with the expected intrinsic gain factor obtained when utilizing flow through a channel, pore or receptor have attracted the attention of scientists working in multidisciplinary fields. However, for the development of implementable biosensors, lab-on-a-chip and microfluidic devices challenging technical problems such as the fabrication of stable lipid membranes, the incorporation of a functional enzyme or receptor into these architectures, and the marriage of the modified membrane to a physical transducer need to be solved. Recently critical endeavours and new discoveries in this scientific field have been achieved and thus, highly sensitive membrane protein-based biosensors are having an increasing impact on drug screening, modern medical care and diagnostics, food safety, environmental monitoring, and biowarfare control.

Prof. Dr. Bernhard Schuster
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


Keywords

  • bioinspired materials
  • biosensing platforms
  • cell-based biosensor
  • functional supported lipid membranes
  • lab-on-a-chip
  • liposomes and proteoliposomes
  • membrane protein-based biosensors
  • membrane-active peptides
  • pharmaceutical screening
  • (trans)membrane proteins

Related Special Issue

Published Papers (4 papers)

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Research

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2615 KiB  
Article
Membrane Affinity of Platensimycin and Its Dialkylamine Analogs
by Ian Rowe, Min Guo, Anthony Yasmann, Abigail Cember, Herman O. Sintim and Sergei Sukharev
Int. J. Mol. Sci. 2015, 16(8), 17909-17932; https://doi.org/10.3390/ijms160817909 - 04 Aug 2015
Cited by 6 | Viewed by 5552
Abstract
Membrane permeability is a desired property in drug design, but there have been difficulties in quantifying the direct drug partitioning into native membranes. Platensimycin (PL) is a new promising antibiotic whose biosynthetic production is costly. Six dialkylamine analogs of PL were synthesized with [...] Read more.
Membrane permeability is a desired property in drug design, but there have been difficulties in quantifying the direct drug partitioning into native membranes. Platensimycin (PL) is a new promising antibiotic whose biosynthetic production is costly. Six dialkylamine analogs of PL were synthesized with identical pharmacophores but different side chains; five of them were found inactive. To address the possibility that their activity is limited by the permeation step, we calculated polarity, measured surface activity and the ability to insert into the phospholipid monolayers. The partitioning of PL and the analogs into the cytoplasmic membrane of E. coli was assessed by activation curve shifts of a re-engineered mechanosensitive channel, MscS, in patch-clamp experiments. Despite predicted differences in polarity, the affinities to lipid monolayers and native membranes were comparable for most of the analogs. For PL and the di-myrtenyl analog QD-11, both carrying bulky sidechains, the affinity for the native membrane was lower than for monolayers (half-membranes), signifying that intercalation must overcome the lateral pressure of the bilayer. We conclude that the biological activity among the studied PL analogs is unlikely to be limited by their membrane permeability. We also discuss the capacity of endogenous tension-activated channels to detect asymmetric partitioning of exogenous substances into the native bacterial membrane and the different contributions to the thermodynamic force which drives permeation. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors)
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1087 KiB  
Article
Probing Peptide and Protein Insertion in a Biomimetic S-Layer Supported Lipid Membrane Platform
by Samar Damiati, Angelika Schrems, Eva-Kathrin Sinner, Uwe B. Sleytr and Bernhard Schuster
Int. J. Mol. Sci. 2015, 16(2), 2824-2838; https://doi.org/10.3390/ijms16022824 - 27 Jan 2015
Cited by 13 | Viewed by 6223
Abstract
The most important aspect of synthetic lipid membrane architectures is their ability to study functional membrane-active peptides and membrane proteins in an environment close to nature. Here, we report on the generation and performance of a biomimetic platform, the S-layer supported lipid membrane [...] Read more.
The most important aspect of synthetic lipid membrane architectures is their ability to study functional membrane-active peptides and membrane proteins in an environment close to nature. Here, we report on the generation and performance of a biomimetic platform, the S-layer supported lipid membrane (SsLM), to investigate the structural and electrical characteristics of the membrane-active peptide gramicidin and the transmembrane protein α-hemolysin in real-time using a quartz crystal microbalance with dissipation monitoring in combination with electrochemical impedance spectroscopy. A shift in membrane resistance is caused by the interaction of α-hemolysin and gramicidin with SsLMs, even if only an attachment onto, or functional channels through the lipid membrane, respectively, are formed. Moreover, the obtained results did not indicate the formation of functional α-hemolysin pores, but evidence for functional incorporation of gramicidin into this biomimetic architecture is provided. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors)
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Review

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6365 KiB  
Review
Biomimetic Membranes for Multi-Redox Center Proteins
by Renate L. C. Naumann, Andreas F. Geiss, Christoph Steininger and Wolfgang Knoll
Int. J. Mol. Sci. 2016, 17(3), 330; https://doi.org/10.3390/ijms17030330 - 03 Mar 2016
Cited by 6 | Viewed by 5419
Abstract
His-tag technology was applied for biosensing purposes involving multi-redox center proteins (MRPs). An overview is presented on various surfaces ranging from flat to spherical and modified with linker molecules with nitrile-tri-acetic acid (NTA) terminal groups to bind his-tagged proteins in a strict orientation. [...] Read more.
His-tag technology was applied for biosensing purposes involving multi-redox center proteins (MRPs). An overview is presented on various surfaces ranging from flat to spherical and modified with linker molecules with nitrile-tri-acetic acid (NTA) terminal groups to bind his-tagged proteins in a strict orientation. The bound proteins are submitted to in situ dialysis in the presence of lipid micelles to form a so-called protein-tethered bilayer lipid membrane (ptBLM). MRPs, such as the cytochrome c oxidase (CcO) from R. sphaeroides and P. denitrificans, as well as photosynthetic reactions centers (RCs) from R. sphaeroides, were thus investigated. Electrochemical and surface-sensitive optical techniques, such as surface plasmon resonance, surface plasmon-enhanced fluorescence, surface-enhanced infrared absorption spectroscopy (SEIRAS) and surface-enhanced resonance Raman spectroscopy (SERRS), were employed in the case of the ptBLM structure on flat surfaces. Spherical particles ranging from µm size agarose gel beads to nm size nanoparticles modified in a similar fashion were called proteo-lipobeads (PLBs). The particles were investigated by laser-scanning confocal fluorescence microscopy (LSM) and UV/Vis spectroscopy. Electron and proton transfer through the proteins were demonstrated to take place, which was strongly affected by the membrane potential. MRPs can thus be used for biosensing purposes under quasi-physiological conditions. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors)
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2012 KiB  
Review
Genetically Encoded Voltage Indicators in Circulation Research
by Lars Kaestner, Qinghai Tian, Elisabeth Kaiser, Wenying Xian, Andreas Müller, Martin Oberhofer, Sandra Ruppenthal, Daniel Sinnecker, Hidekazu Tsutsui, Atsushi Miyawaki, Alessandra Moretti and Peter Lipp
Int. J. Mol. Sci. 2015, 16(9), 21626-21642; https://doi.org/10.3390/ijms160921626 - 08 Sep 2015
Cited by 19 | Viewed by 10907
Abstract
Membrane potentials display the cellular status of non-excitable cells and mediate communication between excitable cells via action potentials. The use of genetically encoded biosensors employing fluorescent proteins allows a non-invasive biocompatible way to read out the membrane potential in cardiac myocytes and other [...] Read more.
Membrane potentials display the cellular status of non-excitable cells and mediate communication between excitable cells via action potentials. The use of genetically encoded biosensors employing fluorescent proteins allows a non-invasive biocompatible way to read out the membrane potential in cardiac myocytes and other cells of the circulation system. Although the approaches to design such biosensors date back to the time when the first fluorescent-protein based Förster Resonance Energy Transfer (FRET) sensors were constructed, it took 15 years before reliable sensors became readily available. Here, we review different developments of genetically encoded membrane potential sensors. Furthermore, it is shown how such sensors can be used in pharmacological screening applications as well as in circulation related basic biomedical research. Potentials and limitations will be discussed and perspectives of possible future developments will be provided. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors)
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