Abstract
Membrane proteins account for approximately one third of all proteins in eukaryotic and prokaryotic cells. These proteins are critical in a diverse array of cellular functions. Despite their obvious importance, the effectiveness of research tools to study the structure and function of integral membrane proteins lags behind that of water-soluble proteins. This is due in part to the lack of probing agents that can specifically and selectively recognize these targets. This review focuses on methods developed to overcome the obstacles of studying membrane proteins. We describe TM protein properties as well as biophysical properties of amino acids within the membrane bilayer. We also summarize the known characteristics of membrane regions in their distinctive environments and generate a summary of current research approaches that succeed in probing interactions of TM proteins within their native setting. This allows further insight into protein-protein interactions in a hydrophobic environment as it pertains to drug development.
Keywords: Integral membrane proteins, protein-protein interactions, peptide, rational drug design, transmembrane domains
Current Pharmaceutical Design
Title: Development of Agents that Modulate Protein-Protein Interactions in Membranes
Volume: 16 Issue: 9
Author(s): Tina X. Zhao, Alexander J. Martinko, Vy H. Le, Jing Zhao and Hang Yin
Affiliation:
Keywords: Integral membrane proteins, protein-protein interactions, peptide, rational drug design, transmembrane domains
Abstract: Membrane proteins account for approximately one third of all proteins in eukaryotic and prokaryotic cells. These proteins are critical in a diverse array of cellular functions. Despite their obvious importance, the effectiveness of research tools to study the structure and function of integral membrane proteins lags behind that of water-soluble proteins. This is due in part to the lack of probing agents that can specifically and selectively recognize these targets. This review focuses on methods developed to overcome the obstacles of studying membrane proteins. We describe TM protein properties as well as biophysical properties of amino acids within the membrane bilayer. We also summarize the known characteristics of membrane regions in their distinctive environments and generate a summary of current research approaches that succeed in probing interactions of TM proteins within their native setting. This allows further insight into protein-protein interactions in a hydrophobic environment as it pertains to drug development.
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Cite this article as:
Zhao X. Tina, Martinko J. Alexander, Le H. Vy, Zhao Jing and Yin Hang, Development of Agents that Modulate Protein-Protein Interactions in Membranes, Current Pharmaceutical Design 2010; 16 (9) . https://dx.doi.org/10.2174/138161210790963878
DOI https://dx.doi.org/10.2174/138161210790963878 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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