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Compounding of elastin poly penta peptide to collagen analog a potential elastomeric prosthetic material



Compounding of elastin poly penta peptide to collagen analog a potential elastomeric prosthetic material



Biomaterials Medical Devices & Artificial Organs 9(3): 181-194



The polypentapeptide, H-(L .cntdot. Val1-L .cntdot. Pro2-Gly3-L .cntdot. Val4-Gly5)n-L .cntdot. 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 analog, 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. 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 EM which demonstrated the importance of a fabric weave with a uniform extension. Irradiation cross-linking has the advantage of being able to produce larger quantities of elastomeric material and compounding to a collagen analog provides the required strength.

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Accession: 005024178

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PMID: 6460533


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