Compounding of elastin polypentapeptide to collagen analogue: a potential elastomeric prosthetic material.
The polypentapeptide, H-(L . Val1-L . Pro2-Gly3-L . Val4-Gly5)n-L . Val-OMe, which is the most common recurring sequence within the elastic fiber, is demonstrated to be elastomeric when irradiation cross-linked but to have limited strength. On irradiation compounding with a collagen analogue, such as Dacron, stress-strain studies show the product to have an elastic modulus greater than that of fibrous aortic elastin and similar to that of aortic wall. In addition, the compounded product has the requisite strength. Of the 40, 50 and 60 MRAD cross-linked polypentapeptide-Dacron products, those derived from the larger doses of 50 and 60 MRAD exhibited somewhat better elastomeric properties. The unstretched and stretched products were characterized by scanning electron microscopy which demonstrated the importance of a fabric weave with a uniform extension. In general irradiation cross-linking has the advantage of being able to produce larger quantities of elastomeric material and compounding to a collagen analogue provides the required strength.
D003094:Collagen; D004548:Elasticity; D004549:Elastin; D008855:Microscopy, Electron, Scanning; D010455:Peptides; D011093:Polyethylene Terephthalates; D011474:Prosthesis Design; D013314:Stress, Mechanical
D010455:Peptides; D011093:Polyethylene Terephthalates; C033943:elastin polypentapeptide; D003094:Collagen; D004549:Elastin