Generic placeholder image

Current Pharmaceutical Design


ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Development of Agents that Modulate Protein-Protein Interactions in Membranes

Author(s): Tina X. Zhao, Alexander J. Martinko, Vy H. Le, Jing Zhao and Hang Yin

Volume 16, Issue 9, 2010

Page: [1055 - 1062] Pages: 8

DOI: 10.2174/138161210790963878

Price: $65


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

Rights & Permissions Print Export Cite as
© 2023 Bentham Science Publishers | Privacy Policy