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A fluorometric study of the interaction of bradykinin with lipids.

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Title A fluorometric study of the interaction of bradykinin with lipids.
 
Creator Appu Rao, A. G.
Setwart, J. M.
Vavrek, R. J.
Sillerud, L. O.
Fink, N. H.
Cann, J. R.
 
Subject 25 Peptide Chemistry
 
Description The interaction of bradykinin (BK) with lipids has been followed by steady-state fluorescence measurements. Addition
of either cerebroside sulfate (CS) or phosphatidylinositol (PI), solubilized with the nonionic surfactant C12E8, to BK or
its analogue [Gly6].BK enhances the relative fluorescence intensity of peptide emission at 288 nm. Fiuorometric
titration of the peptide with lipid has been used to quantitate the interactions in terms of stoichiometry and equilibrium
constant. Job's method of continuous variation for the BK-CS interaction gave a stoichiometry of 1: 2 for the complex.
The value of the equilibrium constant, K, for the interaction of either BK or [Gly61-BK with CS is 1.5.10 4 M-l. The
BK-PI interaction is weaker; K-5.0- 103 M-I. Although electrostatic forces no doubt play a major role in these
interactions, measurements on the model poptide Giy-Phe-Giy indicate that the phenylalanine residues of BK are
disposed in the hydrophobic environment provided by the lipid-C12E8 mixed micelle. 13C-NMR measurements on [99%
t3Ce-Gly6]-BK show that there is no change in its e/s/trans ratio upon interaction with CS. The increase in the relative
fluorescence intensity of BK accompanying its cooperative interaction with sodium dodecyl sulfate (SDS) implicates the
role of hydrophobic forces in this interaction as well. These results bear on the interpretation of the changes in circular
dichroism (CD) of BK caused by SDS.
 
Date 1989
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/2465/1/Biochimica%20et%20Biophysica%20Acta%2C%20997%20%281989%29%20278-283.pdf
Appu Rao, A. G. and Setwart, J. M. and Vavrek, R. J. and Sillerud, L. O. and Fink, N. H. and Cann, J. R. (1989) A fluorometric study of the interaction of bradykinin with lipids. Biochimica et Biophysica Acta, 997. pp. 278-283.