In vitro interactions of opioid peptides with phospholipids. II. Additional spectral evidence.
The interaction of leu-enkephalin with phosphatidylserine has been studied with ultraviolet and circular dichroism spectroscopy methods as well as with fluorescence anisotropy techniques. The data reported hereunder confirm the existence of binding between the two species, and also support the hypothesis that not only the tyrosine, but also the phenylalanine residue in the leu-enkephalin molecule is involved in peptide-lipid interaction. In addition, ultraviolet and CD evidence, taken together, tend to suggest that both aromatic residues are bound, with a different degree of involvement, to the same region of the lipid molecule. The data reported are discussed in terms of the interaction model previously proposed by us.
D001665:Binding Sites; D002942:Circular Dichroism; D004743:Enkephalin, Leucine / Q000378:metabolism*; D005454:Fluorescence Polarization; D008081:Liposomes / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D014443:Tyrosine / Q000378:metabolism
D008081:Liposomes; D010718:Phosphatidylserines; D014443:Tyrosine; D010649:Phenylalanine; D004743:Enkephalin, Leucine