Abstract:
: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.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Lauvrak V,Brekke OH,Ihle O,Lindqvist BHdoi
10.1515/bchm.1997.378.12.1509subject
Has Abstractpub_date
1997-12-01 00:00:00pages
1509-19issue
12eissn
1431-6730issn
1437-4315journal_volume
378pub_type
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