期刊
PLASTIC AND RECONSTRUCTIVE SURGERY
卷 148, 期 6S, 页码 32S-38S出版社
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/PRS.0000000000008784
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Recombinant human type I collagen, which is structurally and functionally identical to human type I collagen, has been successfully expressed and extracted from genetically modified tobacco plants. Unlike tissue-extracted protein, rhCollagen is non-immunogenic and non-allergenic, with an intact triple helix structure displaying superior biological functionality. A photocurable rhCollagen has been developed through chemical modification, allowing cross-linking under illumination at various wavelengths while maintaining its structural and biological functions. The potential applications of this photocurable rhCollagen in aesthetic medicine, particularly as a dermal filler and a bioink for 3D-printed breast implants, are discussed.
Recombinant human type I collagen, identical in structure and functionality to human type I collagen, was successfully expressed and extracted from genetically modified tobacco plants. Contrarily to tissue extracted protein, rhCollagen is not immunogenic and not allergenic and has an intact triple helix structure showing superior biological functionality. A photocurable rhCollagen was developed by chemically modifying the protein to allow cross-linking under illumination at various wavelengths, maintaining the protein structural and biological functions. The use of the photocurable rhCollagen in aesthetic medicine, especially as a dermal filler and as a bioink for 3D-printed breast implant is discussed in this article.
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