Abstract: A vascular prosthetic material having at least one layer containing an elastomeric material capable of reversibly contracting and relaxing by an inverse temperature transition.The vascular prosthetic material matches the compliance and elasticity of vessels replaced, and is biocompatible and biodegradable. The material may also have incorporated therein chemotactic peptides and cell attachment sequences.

Abstract: The invention relates to a mechanochemical engine capable of converting chemical work to mechanical work. The mechanochemical engine comprises an elastomeric material capable of reversibly contracting and relaxing by an inverse temperature transition induced by changes in the chemical potential of a surrounding medium. Examples of elastomeric materials and their elastomeric units that may be used in the mechanochemical engine are described.

Abstract: An elastomeric material, capable of reversibly contracting and relaxing by an inverse temperature transition, in a form suitable for use as a protective layer between a mammalian repair site and a second tissue site whereby adhesion involving said repair site and said second tissue site is substantially prevented.

Abstract: A composition that expands against an exerted pressure, which comprises a polymeric material having an inverse temperature transition in the range of liquid water, wherein at least a fraction of the monomers in the polymer contain a hydrophobic group that is present in an amount sufficient to provide PdV/dS for the polymer of at least 0.2.degree. K. The composition can be used in a variety of different application to produce mechanical work or cause chemical changes in a sealed environment by varying the pressure on the composition, with the degree of mechanical or chemical change being controlled by selection of the number, hydrophobicity, and size of the hydrophobic group and the presence or absence of reactive functional groups in the polymer.

Abstract: A mechanochemical engine capable of desalinating sea water or brackish water by the conversion of mechanical work to chemical work, which comprises: a) a housing containing an elastomeric material capable of being stretched, to thereby allow salt-diminished water to move into the elastomeric material, while substantially repelling solvated salt ions from entry thereto, b) means for stretching and relaxing said elastomeric material in said housing, in connection with said elastomeric material; and c) means for uptake of said sea water or brackish water into said housing, means for draining concentrated salt water from said housing, and means for draining desalinated water from said housing.

Abstract: A polynonapeptide of the formula:--X--(.alpha..beta..gamma..delta..epsilon..theta..lambda..pi..rho.).sub.n Y--wherein:.alpha. is a peptide-forming residue of L-Valine or another peptide-forming residue capable of functioning in position i of a .beta.-turn in a polypeptide;.beta. is a peptide-forming residue of L-Proline or another peptide-forming residue capable of functioning in position i+1 of a .beta.-turn in a polypeptide;.gamma. is a peptide-forming residue of L-Glycine or another peptide-forming residue capable of functioning in position i+2 of a .beta.-turn in a polypeptide;.delta. is a peptide-forming residue of L-Phenylalanine or another peptide-forming residue capable of functioning in position i+3 of a .beta.-turn in a polypeptide;.epsilon. is a peptide-forming residue of Glycine, or D-Alanine, when functioning as position i' of a subsequent .beta.-turn in a polypeptide when .delta. is as defined, or .epsilon. is as defined for .alpha. when .delta. is Glycine or D-Alanine;.theta.

Abstract: A mechanochemical engine cpaable of desalinating sea water or brackish water by the conversion of mechanical work to chemical work, which comprises: a) a housing containing an elastomeric material capable of being stretched, to thereby allow salt-diminished water to move into the elastomeric material, while substantially repelling solvated salt ions from entry thereto, b) means for stretching and relaxing said elastomeric material in said housing, in connection with said elastomeric material; and c) means for uptake of said sea water or brackish water into said housing, means for draining concentrated salt water from said housing, and means for draining desalinated water from said housing.

Abstract: A method of stimulating chemotaxis toward a prosthetic device is disclosed, which method comprises incorporating a chemotactic peptide of the formulaB.sup.1 -X-(AGVPGLGVG).sub.n -(AGVPGFGVG).sub.m -Y-B.sup.2whereinA is a peptide-forming residue of L-alanine;P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine;F is a peptide-forming residue of L-phenylalanine;L is a peptide-forming residue of L-leucine;B.sup.1 is H or a biocompatible N-terminal group;B.sup.2 is OH, OB.sup.3 where B.sup.

Abstract: A bioelastomer containing repeating units comprising elastomeric tetrapeptide or pentapeptide units or a mixture thereof, wherein said repeating units comprise amino acid residues selected from the group consisting of hydrophobic amino acid residues and glycine residues, wherein said repeating units exist in a .beta.-turn which comprises a polypentapeptide unit of the formula:--.alpha.P.rho..OMEGA.G--.sub.nwherein P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; .alpha. is a peptide-forming residue of L-valine or an ionizable peptide-forming residue selected from the group consisting of residues of L-Glu, L-Asp, L-His, L-Lys and L-Tyr; .rho. is a peptide-forming residue of glycine or a peptide-forming residue of D-Glu, D-Asp, D-His, D-Lys and D-Tyr; and .OMEGA.

Abstract: A method of increasing the modulus of elasticity of a biopolymer is disclosed, which comprises incorporating a hexameric unit of the formula--X--(APGVGV).sub.n --Y--whereinA is a peptide-forming residue of L-alanine;P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine;X is PGVGV, GVGV, VGV, GV, V, or a covalent bond;Y is APGVG, APGV, APG, AP, A, or a covalent bond; andn is an integer from 2 to 200, wherein said hexameric unit comprises at least 18 amino acid residues, into an elastomeric polypeptide chain.

Abstract: A bioelastomer containing elastomeric units comprising tetrapeptide, or pentapeptide or units thereof modified by hexapeptide repeating units and mixtures thereof, wherein said repeating units comprise amino acid residues selected from the group consisting of hydrophobic amino acid and glycine residues, wherein said repeating units exist in a conformation having a .beta.-turn which comprises a polypentapeptide unit of the formula:--X.sup.1 --(IPGVG).sub.n --Y.sup.1 --whereinI is a peptide-forming residue of L-isoleucine;P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine; andwherein X.sup.1 is PGVG, GVG, VG, G or a covalent bond; Y.sup.1 is IPGV, IPG, IP, I or a covalent bond; and n is an integer from 1 to 200, or n is 0, with the proviso that X.sup.1 and Y.sup.

Abstract: A method of stimulating chemotaxis toward a prosthetic device is disclosed, which method comprises incorporating a chemotactic peptide of the formulaB.sup.1 -X-(AGVPGFGVG).sub.n -Y-B.sup.2whereinA is a peptide-forming residue of L-alanine:P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine;F is a peptide-forming residue of L-phenylalanine;B.sup.1 is H or a biocompatible N-terminal group;B.sup.2 is OH, OB.sup.3 where B.sup.3 is a non-toxic metal ion, or a biocompatible C-terminal group:X is GVPGFGVG, VPGFGVG, PGFGVG, GFGVG, FGVG, GVG, VG, G or a covalent bond;Y is AGVPGFGV, AGVPGFG, AGVPGF, AGVPG, AGVP, AGV, AG, A or a covalent bond; andn is an integer from 1 to 100;into a surface of the prosthetic device. Prosthetic devices which have the property of enhancing invasion of elastic fiber synthesizing fibroblasts as a result of the chemotactic peptide are also disclosed.

Abstract: A method of stimulating chemotaxis toward a prosthetic device is disclosed, which method comprises incorporating a chemotactic peptide of the formulaB.sup.1 -X-(APGVGV).sub.n -Y-B.sup.2whereinA is a peptide-forming residue of L-alanine;P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine;B.sup.1 is H or a biocompatible N-terminal group;B.sup.2 is OH, OB.sup.3 where B.sup.3 is a non-toxic metal ion, or a biocompatible C-terminal group;X is PGVGV, GVGV, VGV, GV, V, or a covalent bond;Y is APGVG, APGV, APG, AP, A, or a covalent bond; andn is an integer from 1 to 100;into a surface of the prosthetic device. Prosthetic devices which have the property of enhancing invasion of elastic fiber synthesizing fibroblasts as a result of the chemotactic peptide are also disclosed.

Abstract: A method of repairing a natural elastic system in a human or animal body, which comprises replacing a damaged portion of the system with a shaped artificial elastomeric copolymer comprising an elastomeric component selected from the group consisting of tetrapeptide and pentapeptide repeating units or mixtures thereof wherein the repeating units comprise amino acid residues selected from the group consisting of hydrophobic amino acid and glycine residues and the repeating units exist in a conformation having a .beta.-turn and a crosslinking component selected from the group consisting of amino acid and peptide residues of the formula ##STR1## wherein .alpha. represents a covalent bond or a peptide fragment containing 1-10 .alpha.

Abstract: An elastomeric material comprising an elastomeric polypeptide, where the polypeptide comprises pentapeptide repeating units formed of amino acid residues selected from the group consisting of hydrophobic amino acid and glycine residues where the third amino acid residue of at least one repeating unit of the polypeptide has the D configuration if the remaining hydrophobic amino acids have the L configuration or the L configuration if the remaining hydrophobic amino acid residues have the D configuration and where the repeating units exist in a conformation having a .beta.-turn. Also disclosed are elastomeric fabrics formed from the elastomeric material and composites containing it and the use of such fabrics in vascular prosthesis, as well as a method of forming such elastomeric materials.

Abstract: An elastomeric composite material formed from an artificial core fiber and an elastomeric polypeptide chemically bonded to the surface of the core fiber, where the polypeptide comprises tetrapeptide or pentapeptide repeating units or mixtures thereof, the repeating units comprise hydrophobic amino acid or glycine residues, and the amino acid residues of a given repeating unit exist in a conformation having a .beta.-turn. Also disclosed are elastomeric fabrics formed from the elastomeric composite and the use of such fabrics in vascular prosthesis, as well as a method of forming such elastomeric composite materials.

Abstract: An insoluble cross-linked polypentapeptide is totally synthesized by preparing two modified linear polypentapeptides patterned on the polypentapeptide from the pentapeptide (Val.sub.1 -Pro.sub.2 -Gly.sub.3 -Val.sub.4 -Gly.sub.5) one of the repeating peptide sequences contained in tropoelastin, the precursor protein of the core of the elastic fiber of the vascular wall, and by cross-linking the modified polypentapeptides. One of the intermediate polypentapeptides is modified by replacing a portion of at least one of the amino acid residues with the residue of an amino acid having more than one amino function and the other is modified by replacing a portion of at least one of the amino acid residues with the residue of an amino acid having more than one carboxyl function, to provide free amino groups on the one intermediate and free carboxyl groups on the other for interreaction in the presence of a suitable cross-linking agent.

Abstract: An insoluble cross-linked polypentapeptide is totally synthesized by preparing two modified linear polypentapeptides patterned on the polypentapeptide from the pentapeptide (Val.sub.1 -Pro.sub.2 -Gly.sub.3 -Val.sub.4 -Gly.sub.5) one of the repeating peptide sequences contained in tropoelastin, the precursor protein of the core of the elastic fiber of the vascular wall, and by cross-linking the modified polypentapeptides. One of the intermediate polypentapeptides is modified by replacing a portion of at least one of the amino acid residues with the residue of an amino acid having more than one amino function and the other is modified by replacing a portion of at least one of the amino acid residues with the residue of an amino acid having more than one carboxyl function, to provide free amino groups on the one intermediate and free carboxyl groups on the other for interreaction in the presence of a suitable cross-linking agent.