image: THE STRUCTURE AND FUNCTION OF RECOMBINANT HUMANIZED TYPE III COLLAGEN AS WELL AS ITS RELATED PRODUCT approved by CHINA NMPa for COSMETICS USE (ADAPTED FROM THE AUTHORS’ PUBLICATION IN Biochemical and Biophysical Research Communications 2019; 508: 1018-1023).
Credit: Chen, C., et al
Recombinant collagen is divided into recombinant human collagen, recombinant humanized collagen and recombinant collagen-like proteins. Recombinant human collagen refers to recombinant proteins that contain either full-length or partial gene sequences, including at least all helical domains, and encode specific types of human collagen produced by DNA recombinant technology in a manner that reflects the physicochemical and biological functions of collagen protein with triple-helix structure.
Meanwhile, recombinant humanized collagen, classified into class A and B, is a full-length or partial amino acid sequence fragment encoded by a specific type of human collagen gene, or a combination of functional fragments containing human collagen, and prepared by DNA recombination technology.
In particular, class A recombinant humanized collagen contains no non-human protein sequence, while class B recombinant humanized collagen contains non-human protein sequence in its intramolecular linkers and/or tag. Most recent study has shown that class A, but not class B, recombinant humanized collagen possesses triple helix structure as determined by CD spectral analysis.
“Class A recombinant humanized collagen exhibits significantly better biological activities, including the activity of cell adherence, cell migration, and cell proliferation than Class B recombinant humanized collagen,” explains Shibo Jiang, corresponding author of a review published in the Journal of Dermatologic Science and Cosmetic Technology. “Recombinant collagen-like protein is an amino acid sequence, or fragment thereof, encoded by a specific gene, or a combination of such functional amino acid sequence fragments, prepared by DNA recombinant collagen technology. Its gene-encoded amino acid sequence has low homology with the gene-encoding sequence of human collagen.”
A critical functional domain (Gly483-Pro512) was previously identified in human collagen type III (hCOL3A1), which contains multiple charged residues and representative Glu-Lys-Gly and Glu-Arg-Gly charged triplets that play important roles in collagen binding and recognition.
“We noted that the synthetic peptide (C1P) derived from this domain exhibited strong activity through integrin-mediated peptide-membrane interaction and solved crystal structure (a high-resolution of 1.50 Å) of a triple helix formed by C1P with a bending angle of 164.88o,” adds Jiang.
Further, a 480aa recombinant protein consisting of 16 tandem repeats of C1P, designated T16 was developed. It was found that T16 had much higher cell adhesion activity than single C1P peptide or type I human collagen control without cytotoxicity.
“This T16 protein was later defined as a recombinant humanized type III collagen (hCoLIII). A lyophilized fiber product consisting of this recombinant humanized type III collagen developed by Shanxi Jinbo Bio-Pharmaceutical Co., Ltd. (Taiyuan, Shanxi Province, China) was approved by China National Medical Products Administration as an injectable product (class III medical device) for cosmetic use,” shares Jiang.
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Contact author: Dr. Shibo Jiang, Shanghai Medical College, Fudan University, Shanghai 200032, China. Shibojiang@fudan.edu.cn
Journal
Journal of Dermatologic Science and Cosmetic Technology
Method of Research
Literature review
Subject of Research
Not applicable
Article Title
An overview of progress in the application of recombinant collagen in cosmetics
COI Statement
The authors declare no competing interest.