Incorporation of the antimicrobial protein seminalplasmin into lipid bilayer membranes.
The interaction between seminalplasmin, an antimicrobial protein from bull semen, and lipid bilayers has been investigated. The fluorescence of the single tryptophan residue of the protein was measured. In the presence of phosphatidylcholine or phosphatidic acid bilayer vesicles the fluorescence maximum was shifted to shorter wavelengths, indicating transfer of the tryptophan to a more apolar environment. Circular dichroism spectra show an increased alpha-helical content for the protein in the presence of lipid. Quenching experiments clearly show the incorporation of the protein with the tryptophan localized near the bilayer surface. The shift of the tryptophan fluorescence emission was used to monitor the lipid phase transition in phosphatidylcholine membranes.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D008051:Lipid Bilayers; D008297:Male; D029584:Prostatic Secretory Proteins; D011487:Protein Conformation; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D012661:Semen; D029589:Seminal Plasma Proteins; D013050:Spectrometry, Fluorescence
D008051:Lipid Bilayers; D029584:Prostatic Secretory Proteins; D011506:Proteins; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein