The apolipoprotein B3304–3317 peptide as an inhibitor of the lipoprotein (a):apolipoprotein B-containing lipoprotein interaction
| Autor: | W J McConathy, U Olsson, V N Trieu |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Immunodiffusion
Proline Apolipoprotein B Stereochemistry Molecular Sequence Data Peptide Context (language use) Binding Competitive digestive system Biochemistry Chromatography Affinity Kringles Humans Amino Acid Sequence Molecular Biology Apolipoproteins B chemistry.chemical_classification alpha-2-Antiplasmin Binding Sites Sequence Homology Amino Acid biology Chemistry nutritional and metabolic diseases Cell Biology Lipoprotein(a) Ligand (biochemistry) Peptide Fragments Recombinant Proteins Depression Chemical biology.protein lipids (amino acids peptides and proteins) Sequence Alignment Research Article Protein Binding Binding domain Lipoprotein |
| Zdroj: | Biochemical Journal. 307:17-22 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3070017 |
| Popis: | Lipoprotein (a) [Lp(a)] is a risk factor for coronary artery disease. It is characterized by apolipoprotein (a) [apo(a)] disulphide linked to apolipoprotein B (apoB), by Cys4057 of apo(a) and possibly Cys3734 of apoB. We call this the covalent apo(a):apoB-Lp interaction, to distinguish it from the non-covalent Lp(a):apoB-Lp interaction, mediated by the proline-binding kringle-4-like domain(s) of Lp(a). The Lp(a):apoB-Lp interaction was inhibited by an apoB peptide spanning residues 3304-3317. This peptide was found by a computerized search for sites on apoB similar to the plasminogen's kringle-4-binding site of alpha 2-antiplasmin. It probably constitutes part of the Lp(a)-binding site on apoB because: (1) it corresponds to the alpha 2-antiplasmin minimum binding domain for plasminogen's kringle-4; (2) the competitive nature of inhibition [KI = (1.5 +/- 0.7) x 10(-4) M, n = 5] suggested that it and apoB-Lp bound to Lp(a) by the same mechanism at the same site; and (3) it specifically bound Lp(a) and not apoB-Lp, and the bound Lp(a) was dissociated by inhibitors of the Lp(a):apoB-Lp interaction, 6-aminohexanoic acid and L-proline. Inhibition was independent of its proline residue, suggesting that proline in the context of a peptide is not a ligand for the kringle(s) which mediated the binding of Lp(a) to apoB-Lp. |
| Databáze: | OpenAIRE |
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