Identification of a human type XVII collagen fragment with high capacity for maintaining skin health
Collagen XVII (COL17) is a transmembrane protein that mediates skin homeostasis. Due to expression of full length collagen was hard to achieve in microorganisms, arising the needs for selection of collagen fragments with desired functions for microbial biosynthesis. Here, COL17 fragments (27–33 amin...
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KeAi Communications Co., Ltd.
2024-12-01
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| Series: | Synthetic and Systems Biotechnology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405805X24000905 |
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| author | Xinglong Wang Shuyao Yu Ruoxi Sun Kangjie Xu Kun Wang Ruiyan Wang Junli Zhang Wenwen Tao Shangyang Yu Kai Linghu Xinyi Zhao Jingwen Zhou |
| author_facet | Xinglong Wang Shuyao Yu Ruoxi Sun Kangjie Xu Kun Wang Ruiyan Wang Junli Zhang Wenwen Tao Shangyang Yu Kai Linghu Xinyi Zhao Jingwen Zhou |
| author_sort | Xinglong Wang |
| collection | DOAJ |
| description | Collagen XVII (COL17) is a transmembrane protein that mediates skin homeostasis. Due to expression of full length collagen was hard to achieve in microorganisms, arising the needs for selection of collagen fragments with desired functions for microbial biosynthesis. Here, COL17 fragments (27–33 amino acids) were extracted and replicated 16 times for recombinant expression in Escherichia coli. Five variants were soluble expressed, with the highest yield of 223 mg/L. The fusion tag was removed for biochemical and biophysical characterization. Circular dichroism results suggested one variant (sample-1707) with a triple-helix structure at >37 °C. Sample-1707 can assemble into nanofiber (width, 5.6 nm) and form hydrogel at 3 mg/mL. Sample-1707 was shown to induce blood clotting and promote osteoblast differentiation. Furthermore, sample-1707 exhibited high capacity to induce mouse hair follicle stem cells differentiation and osteoblast migration, demonstrating a high capacity to induce skin cell regeneration and promote wound healing. A strong hydrogel was prepared from a chitosan and sample-1707 complex with a swelling rate of >30 % higher than simply using chitosan. Fed-batch fermentation of sample-1707 with a 5-L bioreactor obtained a yield of 600 mg/L. These results support the large-scale production of sample-1707 as a biomaterial for use in the skin care industry. |
| format | Article |
| id | doaj-art-d6b08f6bcf434e40978bcbc4067be9ef |
| institution | OA Journals |
| issn | 2405-805X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Synthetic and Systems Biotechnology |
| spelling | doaj-art-d6b08f6bcf434e40978bcbc4067be9ef2025-08-20T01:56:23ZengKeAi Communications Co., Ltd.Synthetic and Systems Biotechnology2405-805X2024-12-019473374110.1016/j.synbio.2024.06.001Identification of a human type XVII collagen fragment with high capacity for maintaining skin healthXinglong Wang0Shuyao Yu1Ruoxi Sun2Kangjie Xu3Kun Wang4Ruiyan Wang5Junli Zhang6Wenwen Tao7Shangyang Yu8Kai Linghu9Xinyi Zhao10Jingwen Zhou11Engineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaBloomage Biotechnology Corporation Limited, 678 Tianchen Street, Jinan, Shandong, 250101, ChinaBloomage Biotechnology Corporation Limited, 678 Tianchen Street, Jinan, Shandong, 250101, ChinaBloomage Biotechnology Corporation Limited, 678 Tianchen Street, Jinan, Shandong, 250101, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, ChinaEngineering Research Center of Ministry of Education on Food Synthetic Biotechnology and School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China; Jiangsu Province Engineering Research Center of Food Synthetic Biotechnology, Jiangnan University, Wuxi, 214122, China; School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, 214122, China; Corresponding author. Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.Collagen XVII (COL17) is a transmembrane protein that mediates skin homeostasis. Due to expression of full length collagen was hard to achieve in microorganisms, arising the needs for selection of collagen fragments with desired functions for microbial biosynthesis. Here, COL17 fragments (27–33 amino acids) were extracted and replicated 16 times for recombinant expression in Escherichia coli. Five variants were soluble expressed, with the highest yield of 223 mg/L. The fusion tag was removed for biochemical and biophysical characterization. Circular dichroism results suggested one variant (sample-1707) with a triple-helix structure at >37 °C. Sample-1707 can assemble into nanofiber (width, 5.6 nm) and form hydrogel at 3 mg/mL. Sample-1707 was shown to induce blood clotting and promote osteoblast differentiation. Furthermore, sample-1707 exhibited high capacity to induce mouse hair follicle stem cells differentiation and osteoblast migration, demonstrating a high capacity to induce skin cell regeneration and promote wound healing. A strong hydrogel was prepared from a chitosan and sample-1707 complex with a swelling rate of >30 % higher than simply using chitosan. Fed-batch fermentation of sample-1707 with a 5-L bioreactor obtained a yield of 600 mg/L. These results support the large-scale production of sample-1707 as a biomaterial for use in the skin care industry.http://www.sciencedirect.com/science/article/pii/S2405805X24000905Type XVII collagenHair follicle stem cell differentiationHigher-order assemblyCollagen recombinant expression |
| spellingShingle | Xinglong Wang Shuyao Yu Ruoxi Sun Kangjie Xu Kun Wang Ruiyan Wang Junli Zhang Wenwen Tao Shangyang Yu Kai Linghu Xinyi Zhao Jingwen Zhou Identification of a human type XVII collagen fragment with high capacity for maintaining skin health Synthetic and Systems Biotechnology Type XVII collagen Hair follicle stem cell differentiation Higher-order assembly Collagen recombinant expression |
| title | Identification of a human type XVII collagen fragment with high capacity for maintaining skin health |
| title_full | Identification of a human type XVII collagen fragment with high capacity for maintaining skin health |
| title_fullStr | Identification of a human type XVII collagen fragment with high capacity for maintaining skin health |
| title_full_unstemmed | Identification of a human type XVII collagen fragment with high capacity for maintaining skin health |
| title_short | Identification of a human type XVII collagen fragment with high capacity for maintaining skin health |
| title_sort | identification of a human type xvii collagen fragment with high capacity for maintaining skin health |
| topic | Type XVII collagen Hair follicle stem cell differentiation Higher-order assembly Collagen recombinant expression |
| url | http://www.sciencedirect.com/science/article/pii/S2405805X24000905 |
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