Peptide inhibitors of fibronectin and related collagen-binding proteins
AssigneeThe United States of America as represented by the Department of Health and Human Services
InventorsDavid D. Roberts, Henry C. Krutzsch, John M. Sipes, Neng-hua Guo, Eric Negre
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Abstract
Peptides derived from the second type 1 repeat of human endothelial cell thrombospondin which bind to the gelatin-binding domain of fibronectin have been isolated and synthetically produced. The peptides can be used to bind to fibronectin or other related collagen-binding proteins to inhibit fibronectin-dependent cell adhesion to collagen matrices and to inhibit interactions with collagen of other proteins that share homologies with the gelatin-binding domain of fibronectin.
Claims10
A method for inhibiting fibronectin-dependent cell adhesion, the method comprising administering to a cell dependent upon fibronectin for cell adhesion an effective amount of a composition comprising a peptide having a specific binding affinity for the gelatin-binding domain of fibronectin, said peptide from 3 to 18 amino acids in length and consisting essentially of the sequence (A),
- Xa--Xb--His--Trp--Xc,
- wherein Xa is H or an amino acid sequence of from 1 to 13 amino acids derived from the consecutively occurring thrombospondin amino acid residues 394-420, Xb is serine, alanine, tryptophan, or threonine and Xc is OH, NH.sub.2, or an amino acid sequence of from 1 to 13 amino acids derived from the consecutively occurring human thrombospondin amino acid residues 424-450, and at least one of Xa and Xb includes a tryptophan residue located within three amino acid residues from Trp in sequence (A).
Dependencies are inferred from the claim text.