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Membrane Protein Based Biosensors 2016

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 December 2016) | Viewed by 19223

Special Issue Editor


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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
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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

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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

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Published Papers (2 papers)

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2836 KiB  
Article
A Female-Biased Odorant Receptor from Apolygus lucorum (Meyer-Dür) Tuned to Some Plant Odors
by Zhixiang Zhang, Meiping Zhang, Shuwei Yan, Guirong Wang and Yang Liu
Int. J. Mol. Sci. 2016, 17(8), 1165; https://doi.org/10.3390/ijms17081165 - 28 Jul 2016
Cited by 17 | Viewed by 6414
Abstract
Apolygus lucorum (Meyer-Dür) (Hemiptera: Miridae) is a serious pest of cotton, jujube, grape and many other crops around the world. Understanding how olfactory information directs this insect to its host plants may provide environment-friendly approaches to the control of its population in agriculture. [...] Read more.
Apolygus lucorum (Meyer-Dür) (Hemiptera: Miridae) is a serious pest of cotton, jujube, grape and many other crops around the world. Understanding how olfactory information directs this insect to its host plants may provide environment-friendly approaches to the control of its population in agriculture. In our study, we cloned an odorant receptor gene, AlucOR46, that was specifically expressed in antennae and female-biased. Functional expression of AlucOR46 in Xenopus oocytes showed that it is tuned to six plant volatiles (S)-(−)-Limonene, (R)-(+)-Limonene, (E)-2-Hexenal, (E)-3-Hexenol, 1-Heptanol and (1R)-(−)-Myrtenol. Electroantennogram (EAG) recordings revealed that all six compounds could elicit electrophysiological responses from the antennae of A. lucorum, higher in females. Our results are in agreement with previous reports showing that (E)-2-Hexenal could attract female A. lucorum in behavior experiments. These results suggest that AlucOR46 might play an important role in locating the host plants of A. lucorum and therefore represents a suitable target for green pest control. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors 2016)
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Review

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791 KiB  
Review
Recent Advances in Understanding Amino Acid Sensing Mechanisms that Regulate mTORC1
by Liufeng Zheng, Wei Zhang, Yuanfei Zhou, Fengna Li, Hongkui Wei and Jian Peng
Int. J. Mol. Sci. 2016, 17(10), 1636; https://doi.org/10.3390/ijms17101636 - 29 Sep 2016
Cited by 82 | Viewed by 12341
Abstract
The mammalian target of rapamycin (mTOR) is the central regulator of mammalian cell growth, and is essential for the formation of two structurally and functionally distinct complexes: mTORC1 and mTORC2. mTORC1 can sense multiple cues such as nutrients, energy status, growth factors and [...] Read more.
The mammalian target of rapamycin (mTOR) is the central regulator of mammalian cell growth, and is essential for the formation of two structurally and functionally distinct complexes: mTORC1 and mTORC2. mTORC1 can sense multiple cues such as nutrients, energy status, growth factors and hormones to control cell growth and proliferation, angiogenesis, autophagy, and metabolism. As one of the key environmental stimuli, amino acids (AAs), especially leucine, glutamine and arginine, play a crucial role in mTORC1 activation, but where and how AAs are sensed and signal to mTORC1 are not fully understood. Classically, AAs activate mTORC1 by Rag GTPases which recruit mTORC1 to lysosomes, where AA signaling initiates. Plasma membrane transceptor L amino acid transporter 1 (LAT1)-4F2hc has dual transporter-receptor function that can sense extracellular AA availability upstream of mTORC1. The lysosomal AA sensors (PAT1 and SLC38A9) and cytoplasmic AA sensors (LRS, Sestrin2 and CASTOR1) also participate in regulating mTORC1 activation. Importantly, AAs can be sensed by plasma membrane receptors, like G protein-coupled receptor (GPCR) T1R1/T1R3, and regulate mTORC1 without being transported into the cells. Furthermore, AA-dependent mTORC1 activation also initiates within Golgi, which is regulated by Golgi-localized AA transporter PAT4. This review provides an overview of the research progress of the AA sensing mechanisms that regulate mTORC1 activity. Full article
(This article belongs to the Special Issue Membrane Protein Based Biosensors 2016)
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