The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems.
Ultraviolet-visible spectroscopy has been used as a rapid method to evaluate the hydrophobic interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobic core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobic interaction occurs, a 1-nm bathochromic shift is observed in the uv-visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des-Arg9 bradykinin all exhibited the 1-nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met-enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles.
Young
J K
JK
Department of Chemistry, Mississippi State University, Mississippi State 39762.
Graham
W H
WH
Beard
D J
DJ
Hicks
R P
RP
D000595:Amino Acid Sequence; D008244:Lysophosphatidylcholines; D008566:Membranes / Q000737:chemistry / Q000378:metabolism*; D008823:Micelles; D008954:Models, Biological; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate; D013056:Spectrophotometry, Ultraviolet; D014867:Water / Q000737:chemistry
D008244:Lysophosphatidylcholines; D008823:Micelles; D009479:Neuropeptides; D014867:Water; D012967:Sodium Dodecyl Sulfate