Tetrapeptide
AssigneeLa Jolla Cancer Research Foundation
InventorsErkki Ruoslahti, Michael Pierschbacher
Life of this patent
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Abstract
The peptide X-Arg-Gly-Asp-R-Y wherein X is H or at least one amino acid and Y is OH or at least one amino acid, and R is an amino acid selected from Thr or Cys, or other amino acid, having the same cell-attachent activity as fibronectin and the peptide X-Arg-Gly-Asp-Ser-Y, wherein X and Y, having said activity are disclosed.
Claims11
A method for promoting cell attachment to a substrate comprising the steps of:
- immobilizing on the substrate a non-naturally occurring polypeptide which includes as the cell-attachment-promoting constituent the sequence -Arg-Gly-Asp-R- wherein R is Ser, Cys, Thr or other amino acid such that the polypeptide has cell-attachment-promoting activity;
- and providing free cells for attachment to said substrate,.
A method for promoting cell attachment to a substrate comprising the steps of:
- immobilizing on the substrate a composition of matter comprising a non-naturally occurring peptide
- X-Arg-Gly-Asp-R-Y
- wherein X is H or at least one amino acid and Y is OH or at least one amino acid, and R is an amino acid selected from Ser Thr, Cys or other amino acid, such that said peptide has cell-attachmentpromoting activity;
- and
- providing free cells for attachment to the substrate.
A method of promoting cell attachment activity comprising the steps of:
- immobilizing on a substrate a non-naturally occurring polypeptide including the sequence Arg-Gly-Asp-Ser;
- and
- providing free cells for attachment to said substrate.
A method for promoting cell attachment to a substrate comprising the steps of:
- immobilizing on the substrate a substantially pure peptide including as the cell-attachment-promoting constituent the amino acid sequence Arg-Gly-Asp-R wherein R is Ser, Cys, Thr or other amino acid, said peptide having cell-attachment-promoting activity, and said peptide not being a naturally occurring peptide;
- and
- providing free cells for attachment to said substrate.
A method of promoting cell attachment to a substrate, comprising the steps of:
- immobilizing on the substrate a polypeptide which includes as the cell-attachment-promoting constituent the amino acid sequence Arg-Gly-Asp-R wherein R is Ser, Cys, Thr or other amino acid such that the polypeptide has cell attachment promoting activity, said polypeptide having less than about 31 amino acid residues;
- and
- providing free cells for attachment to said substrate.
A method of prommoting cell attachment to a substrate, comprising the steps of:
- immobilizing on the substrate a composition of matter comprising a substantially pure polypeptide
- X-Arg-Gly-Asp-R-Y
- wherein X is H or at least one amino acid and Y is OH or at least one amino acid, and R is an amino acid selected from Ser, Syc, Thr or other amino acid, said peptide having cell attachment promoting activity, and said peptide not being a naturally occurring peptide;
- and
- providing free cells for attachment to said substrate.
A method of promoting cell attachment to a substrate, comprising the steps of:
- immobilizing on the substrate a composition of matter comprising a polypeptide
- X-Arg-Gly-Asp-R-Y
- wherein X is H or at least one amino acid and Y is OH or at least one amino acid, and R is an amino acid selected from Ser, Cys, Thr or other amino acid such that said peptide has cell attachment promoting activity, said polypeptide having less than about 31 amino acid residues;
- and
- providing free cells for attachment to said substrate.
A substantially pure peptide including as the cell-attachment-promoting constituent the amino acid sequence Arg-Gly-Arg-R wherein R is Ser, Cys, Thr or other amino acid, said peptide having cell-attachmentpromoting activity, and said peptide not being a naturally occurring peptide.
A peptide including as the cell-attachment-promoting constituent the amino acid sequence Arg-Gly-Asp-R, wherein R is Ser, Cys, Thr or other amino acid such that the peptide has cell-attachment-promoting activity, wherein said peptide has less than about 31 amino acid residues.
Dependencies are inferred from the claim text.