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Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2009 Dec; Vol. 1794 (12), pp. 1725-33. Date of Electronic Publication: 2009 Aug 14. - Publication Year :
- 2009
-
Abstract
- The microenvironment and accessibility of the tryptophan residues in domain B of PDC-109 (PDC-109/B) in the native state and upon ligand binding have been investigated by fluorescence quenching, time-resolved fluorescence and red-edge excitation shift (REES) studies. The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein. The degree of quenching achieved by different quenchers with PDC-109/B bound to Lyso-PC and DMPC membranes was significantly higher as compared to the full PDC-109 protein, indicating that membrane binding afforded considerably lesser protection to the tryptophan residues of domain B as compared to those in the full PDC-109 protein. Finally, changes in red-edge excitation shift (REES) seen with PDC-109/B upon binding to DMPC membranes and Lyso-PC micelles were smaller that the corresponding changes in the REES values observed for the full PDC-109. These results, taken together suggest that intact PDC-109 penetrates deeper into the hydrophobic parts of the membrane as compared to domain B alone, which could be the reason for the inability of PDC-109/B to induce cholesterol efflux, despite its ability to recognize choline phospholipids at the membrane surface.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
Cattle
Choline metabolism
In Vitro Techniques
Kinetics
Ligands
Liposomes
Male
Micelles
Molecular Sequence Data
Protein Structure, Tertiary
Seminal Vesicle Secretory Proteins genetics
Spectrometry, Fluorescence
Tryptophan chemistry
Membrane Lipids chemistry
Membrane Lipids metabolism
Phospholipids chemistry
Phospholipids metabolism
Seminal Vesicle Secretory Proteins chemistry
Seminal Vesicle Secretory Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1794
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 19683598
- Full Text :
- https://doi.org/10.1016/j.bbapap.2009.08.010