Self-aligning peptides modeled on human elastin and other fibrous proteins

DETAILED DESCRIPTION OF PREFERRED EMBODIMENTS The present invention is directed to unique polypeptides modeled on human elastin and other naturally occurring fibrous proteins.
While the discussion below often refers to human elastin as the exemplary parent protein, polypeptides modeled on other naturally occurring fibrous proteins are contemplated by the present invention, and can be made and used in manners analogous to those described for polypeptides modeled on human elastin.
The phrase "parent protein" here denotes the protein on which a polypeptide of the invention is modeled.
For example, a polypeptide modeled on human elastin comprises a portion of the human tropoelastin amino acid sequence.
A "naturally occurring fibrous protein" is any fibrous protein found in nature, where the phrase "fibrous protein" has the conventional meaning in the art.
Thus, a fibrous protein is a protein that consists of polypeptide chains arranged in a matrix so as to form long fibers or sheets.
See Lehninger, BIOCHEMISTRY 60 (1975).
Examples of fibrous proteins include, but are not limited to, elastin, lamprin and spider silk protein.
Robson et al.
, J.
Biol.
Chem.
268: 1440-47 (1993), incorporated by reference herein in its entirety, discloses additional proteins on which polypeptides of the present invention may be modeled.
Amino acid sequence information is available for elastin and other fibrous extracellular matrix proteins, such as spider silks and lamprin.
Together with analyses of secondary and tertiary structures, this information has led to general theories concerning their mechanical properties and, in particular, mechanisms for their assembly into insoluble fibers.
Elastin is synthesized in vivo as a monomer called tropoelastin which, upon secretion from the cell, assembles into a branched polymeric network through the formation of covalent crosslinks called desmosines.
Mecham et al.
, in CELL BIOLOGY OF EXTRACELLULAR MATRIX, 2D ED.
(New York, 1991).
Desmosine crosslinks are generated enzymically through the action of lysyl oxidase