Appeal No. 2000-0137 Page 2
Application No.08/646,558
carboxylic acid or amide group; said peptide being a cyclic disulfide
and comprising the amino acid residue sequence of Xaa1-Xaa2-
Asp-Xaa3 (SEQ ID NO:15), where Xaa1, Xaa2 and Xaa3 are each
independently any aromatic or hydrophobic amino acid residue with
the proviso that when Xaa1 is Lys or Arg, Xaa2 cannot be Gly or
Cys.
The examiner relies on the following references:
Lobl et al. (Lobl) 5,192,746 Mar. 09, 1993
Kogan et al. (Kogan) 5,510,332 Apr. 23, 1996
Nutt et al. (Nutt) 0,422,938 Apr. 17, 1991
(European Patent)
Ali et al. (Ali (EP)) 0,341,915 Nov. 15, 1989
(European Patent)
Mould et al. (Mould I), “The CS5 Peptide is a Second Site in the IIICS Region of
Fibronection Recognized by the Integrin α4β1,” Journal of Biological Chemistry,
Vol. 266, No. 6, pp. 3579-3585 (1991)
Mould et al. (Mould II), “Identification of a Novel Recognition Sequence for the
Integrin α4β1 in the COOH-Terminal Heparin-Binding Domain of Fibronectin,”
EMBO Journal, Vol. 10, No. 13, pp. 4089-4095 (1991)
Ali et al. (Ali (Peptides)), ”Structure-Activity Studies Toward the Improvement of
Antiaggregatory Activity of Arg-Gly-Asp-Ser (RGDS),” Peptides: Chemistry,
Structure and Biology (Proceedings of the Eleventh Amer. Pept. Symposium),
pp. 94-96 (1989)
Aumailley et al. (Aumailley) “Arg-Gly-Asp constrained within cyclic
pentapeptides,” FEBS Letters, Vol. 291, No. 1, pp. 50-54 (1991)
Davies et al. (Davies), “Synthetic Peptide Mimics of the Active Domain of
Fibronectin,” Biochemical Society Transactions, Vol. 18, pp. 1326-1328 (1990)
Pierschbacher et al. (Pierschbacher), “Variants of the cell recognition site of
fibronection that retain attachment-promoting activity,” Proc. Natl. Acad. Sci.
USA, Vol. 81, pp. 5985-5988 (1984)
Yamada, “Adhesive Recognition Sequences,” Journal of Biological Chemistry,
Vol. 266, No. 20, pp. 12809-12812 (1991)
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