Evaluation of the membrane-binding properties of the proximal region of the angiotensin II receptor (AT1A) carboxyl terminus by surface plasmon resonance.
The proximal region of the angiotensin II receptor (AT1A) carboxyl-terminus (known as helix VIII) is important for receptor function. In this study, we used surface plasmon resonance (SPR) to examine the interaction of helix VIII-derived peptides with three model lipid membranes. The membrane-binding properties of these synthetic peptides, as well as a series of peptide analogues with modified amino acid sequences, could be explained by both amino acid sequence and kinetic binding data by SPR. The helix VIII peptides showed a higher affinity for lipid membranes that contained negatively charged phospholipid, rather than zwitterionic phospholipid. The findings of an SPR study may be useful for estimating the cooperative binding of intracellular receptor domains with G proteins and the components of the lipid bilayer.
Kamimori
Hiroshi
H
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia. hiroshi.kamimori@shionogi.co.jp
Unabia
Sharon
S
Thomas
Walter G
WG
Aguilar
Marie-Isabel
MI
D002462:Cell Membrane / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry*; D011485:Protein Binding; D044140:Receptor, Angiotensin, Type 1 / Q000737:chemistry* / Q000378:metabolism*; D020349:Surface Plasmon Resonance / Q000379:methods*
D008081:Liposomes; D044140:Receptor, Angiotensin, Type 1