Mechanism of action of preservatives in cosmetics
KeAi Communications Co., Ltd.
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CHEMICAL STRUCTURES OF CMIT (LEFT) AND MIT (RIGHT)
view moreCredit: Zhenyu Tang, et al
Preservatives inhibit or kill microorganisms, preventing spoilage and extending the shelf life of cosmetics. Ideally, preservatives should be effective against a wide range of microorganisms, soluble in water, non-toxic, non-irritating to the skin, stable and effective over a broad temperature range. Importantly, it should not cause discoloration, fading or unpleasant odor in the product.
Additionally, preservatives should have a neutral pH or at least not significantly affect the product’s pH, and should be economically viable and easily accessible. They should also not react with other organic compounds in the formulation.
In a review published in the Journal of Dermatologic Science and Cosmetic Technology, two Chinese researchers looked into the mechanism of action of preservatives in cosmetics.
Co-author Zhenyu Tang, CTO at Henning Chemical (Shanghai) Co., Ltd, says, “The preservatives presented in this review, at normal use levels, kill the microorganisms rather than inhibiting their growth. These substances can affect various substructures of microbial cells, including the cell wall, cell membrane, enzymes involved in metabolism, protein synthesis systems, and genetic material.”
Notably, the effectiveness of a preservative depends on factors such as concentration, exposure time, and the specific microorganism being targeted.
Studying the mechanism of preservatives is important for several reasons.
“It helps in the development of improved preservation methods and the identification of more effective preservatives. Understanding how preservatives work allows for targeted modifications to enhance their antimicrobial properties,” adds Tang.
Further, studying the mechanism of action helps in determining the optimal conditions for the use of preservatives, such as concentration and exposure time, to ensure their effectiveness while minimizing any potential adverse effects.
“Overall, research on preservatives is crucial for monitoring their usage and establishing appropriate detection methods to prevent misuse and potential harm to human health,” says Tang.
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Contact author name, affiliation, email address: Zhenyu Tang, Henning Chemical (Shanghai) Co., Ltd., tzy@henningchem.com
Journal
Journal of Dermatologic Science and Cosmetic Technology
Method of Research
Literature review
Subject of Research
Not applicable
Article Title
Mechanism of action of preservatives in cosmetics
COI Statement
The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Zhenyu Tang and Qiaoyan Du are currently employed by Henning Chemical (Shanghai) Co., Ltd.
Progress in recombinant collagen application in cosmetics
KeAi Communications Co., Ltd.
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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).
view moreCredit: 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
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