Development of agents that modulate protein-protein interactions in membranes.
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.
Zhao
Tina X
TX
University of Colorado Boulder, 215 UCB, Boulder, Colorado 80309, USA.
Martinko
Alexander J
AJ
Le
Vy H
VH
Zhao
Jing
J
Yin
Hang
H
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D016503:Drug Delivery Systems / Q000379:methods*; D015195:Drug Design; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D010455:Peptides / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects*; D054730:Protein Interaction Domains and Motifs / Q000187:drug effects; D025941:Protein Interaction Mapping
D008565:Membrane Proteins; D010455:Peptides