Identification and characterisation of C1q-binding phage displayed peptides
| Autor: | Øistein Ihle, Björn H. Lindqvist, Ole Henrik Brekke, Vigdis Lauvrak |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Phage display
Phagemid Protein subunit Clinical Biochemistry Molecular Sequence Data chemical and pharmacologic phenomena Ligands Biochemistry Mitochondrial Proteins Classical complement pathway Viral Proteins Peptide Library Consensus Sequence Humans Bacteriophages Amino Acid Sequence Binding site Panning (camera) Molecular Biology Membrane Glycoproteins biology Chemistry Complement C1q Complement system Receptors Complement Hyaluronan Receptors Integrin alpha M biology.protein Carrier Proteins Peptides |
| Zdroj: | Biological chemistry. 378(12) |
| ISSN: | 1431-6730 |
| Popis: | Five phage displayed peptide libraries were screened for binders to C1q, the recognition subunit of the classical complement pathway. Two rounds of panning resulted in the isolation and characterisation of several different phage displayed C1q-binding peptides from all five libraries. Two groups of the characterised peptides show sequence similarity with part of the metal ion dependent adhesion site (MIDAS) of integrin A-domains, and the site 187LRNPCPNKEKECQPPF of CD18 (integrin beta2), respectively. These results support binding of complement receptor 3 (CR3, CD11b/CD18, Mac1) to C1q and further suggest C1q binding sites in CR3. We also discuss sequence matches between the characterised peptides and proteins known to interact with C1q, as well as other proteins listed in the SwissProt databank. These findings are of interest for the study of the complement system and may lead to the development of peptides, fusion products or peptido-mimetics with C1q modulating potential. |
| Databáze: | OpenAIRE |
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