The use of UV‐visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems | Zendy

Young John K. | Zendy; Graham William H. | Zendy; Beard Debbie J. | Zendy; Hicks Rickey P. | Zendy

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The use of UV‐visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems

Author(s) -

Young John K.,

Graham William H.,

Beard Debbie J.,

Hicks Rickey P.

Publication year - 1992

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.360320815

Subject(s) - chemistry , bathochromic shift , sodium dodecyl sulfate , micelle , aqueous solution , lysophosphatidylcholine , cationic polymerization , membrane , bradykinin , ultraviolet visible spectroscopy , photochemistry , pulmonary surfactant , spectroscopy , organic chemistry , phospholipid , phosphatidylcholine , biochemistry , physics , receptor , quantum mechanics , fluorescence

Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobia 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‐Arg 9 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. © 1992 John Wiley & Sons, Inc.

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