Conformationally stabilized cell adhesion peptides
AssigneeLa Jolla Cancer Research Institute
InventorsMichael D. Pierschbacher, Erkki I. Ruoslahti
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Abstract
Novel synthetic Arg-Gly-Asp containing peptides which have high affinity and specificity for their receptors by virtue of restrictions on their stereochemical conformation. Such restrictions can be provided by cyclization, by inclusion into a constraining conformational structure such as a helix, by providing an additional chemical structure such as an amide or an enantiomer of a naturally occurring amino acid, or by other methods. In particular, there are provided cyclic peptides having increased affinity and selectivity for the certain receptors over that of linear, Arg-Gly-Asp-containing synthetic peptides.
Claims13
A method of inhibiting binding of a natural ligand to a vitronectin receptor comprising contacting said vitronectin receptor with a cyclic peptide containing the sequence Arg-Gly-Asp, said Arg-Gly-Asp sequence being conformationally restricted, thereby selectively inhibiting binding of said natural ligand to said vitronectin receptor with respect to the function of other receptors.
A method of selectively inhibiting attachment of cells to vitronectin comprising providing to said cells in vitro a solution of a cyclic peptide containing the sequence Arg-Gly-Asp, said Arg-Gly-Asp sequence being conformationally restricted, thereby selectively inhibiting attachment of said cells to said vitronectin.
A method of selectively inhibiting attachment of cells to vitronectin comprising providing to said cells in vivo a solution of a peptide containing the sequence Arg-Gly-Asp, said Arg-Gly-Asp sequence being conformationally restricted, thereby selectively inhibiting attachment of said cells to said vitronectin.
A method of selectively inhibiting binding of vitronectin receptor-containing cells to a substrate comprising providing to said cells in vitro a solution containing a cyclic peptide that encompasses the sequence Arg-Gly-Asp, said Arg-Gly-Asp sequence being conformationally restricted, thereby selectively inhibiting binding of said vitronectin receptor-containing cells to said substrate.
A method of selectively inhibiting binding of vitronectin receptor-containing cells to a substrate comprising providing to said cells in vivo a solution containing a peptide that encompasses the sequence Arg-Gly-Asp, said Arg-Gly-Asp sequence being conformationally restricted, thereby selectively inhibiting binding of said vitronectin receptor-containing cells to said substrate.
A method of selectively inhibiting binding of vitronectin receptor-containing cells to a substrate comprising the steps of:
- a. providing to said cells in vitro a cyclic peptide containing the sequence Arg-Gly-Asp in solution, said Arg-Gly-Asp sequence being conformationally restricted;
- and
- b. contacting said cells with said solution.
A method of selectively inhibiting binding of vitronectin receptor-containing cells to a substrate comprising the steps of:
- a. providing to said cells in vivo a peptide containing the sequence Arg-Gly-Asp in solution, said Arg-Gly-Asp sequence being conformationally restricted;
- and
- b. contacting said cells with said solution.
A method of selectively inhibiting binding of cells to a substrate comprising providing to said cells in vitro a solution of a peptide containing an Arg-Gly-Asp sequence chemically modified with an additional chemical structure, wherein said additional chemical structure conformationally restricts the stereochemical structure of said Arg-Gly-Asp sequence in such a way that the affinity of the Arg-Gly-Asp binding site sequence for a particular receptor is enhanced.
A method of selectively inhibiting binding of cells to a substrate comprising providing to said cells in vivo a solution of a peptide containing an Arg-Gly-Asp sequence chemically modified with an additional chemical structure, wherein said additional chemical structure conformationally restricts the stereochemical structure of said Arg-Gly-Asp sequence in such a way that the affinity of the Arg-Gly-Asp binding site sequence for a particular receptor is enhanced.
Dependencies are inferred from the claim text.