Self-aligning peptides modeled on human elastin and other fibrous proteins
AssigneesProtein Specialties, Ltd., HSC Research and Development Limited Partnership
InventorsAser Rothstein, Fred Keeley, Steven Rothstein
Life of this patent
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Abstract
A polypeptide is provided that has a secondary structure characterized by at least three beta-sheet/beta-turn structures, and that is not a naturally occurring fibrous protein. Such polypeptides, illustrated by one modeled on elastin, are useful in prosthesis.
Claims26
A polypeptide that comprises at least three beta-sheet/beta-turn structures and that is not a naturally occurring fibrous protein.
A material comprising two or more polypeptides selected from the group consisting of:
- (A) a polypeptide consisting essentially of a portion of the amino acid sequence set forth in FIG. 1B comprising at least three beta-sheet/beta-turn structures;
- (B) a polypeptide consisting essentially of a portion of the amino acid sequence of an animal elastin comprising at least three beta-sheet/beta-turn structures;
- (C) a polypeptide consisting essentially of a portion of the amino acid sequence of lamprin comprising at least three beta-sheet/beta-turn structures;
- and
- (D) a polypeptide consisting essentially of a portion of the amino acid sequence of a spider silk protein comprising at least three beta-sheet/beta-turn structures,
- wherein the two or more polypeptides may be the same or different.
A polypeptide having the primary structure of a portion of a naturally occurring fibrous protein and a secondary structure comprising at least three beta-sheet/beta-turn structures, wherein
- (A) each of the beta-sheet/beta-turn structures comprises from 3 to about 7 amino acid residues and (B) the polypeptide is not a naturally occurring fibrous protein.
Dependencies are inferred from the claim text.