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        DNA 기반 금속 나노 와이어의 제작기술

        한경엽 ( Gyeongyeop Han ),이정규 ( Jungkyu K. Lee ) 한국공업화학회 2018 공업화학 Vol.29 No.3

        DNA를 기반으로 한 금속 나노와이어는 전기적인 물성은 떨어지지만, 제작 방식이 간단하고, 대면적에서 대량으로 제작할 수 있으며, 유기 반응을 통해 분자 소자 제작의 기판으로도 사용가능한 차세대 재료로 전망된다. 본 총설에서는 DNA 금속화 반응을 이용한 나노와이어의 제작 및 3차원 구조체의 제작 기술에 대해 소개하고, 이와 관련한 연구현황과 발전 방향에 대해 논의하고자 한다. DNA metallization has been emerged as a candidate for fabricating nanocircuits because of its simple process over a large area on a surface. With unique properties, DNA can be an excellent template to achieve molecular electronics. Thus, we in-troduced the preparation and properties of DNA metallization, and also suggested future directions in this review.

      • KCI등재후보

        Extraction and Characterization of Human Adipose Tissue-Derived Collagen: Toward Xeno-Free Tissue Engineering

        Kim Minseong,Yeo MyungGu,Lee KyoungHo,Park Min-Jeong,Han Gyeongyeop,Lee Chansong,Park Jihyo,Jung Bongsu 한국조직공학과 재생의학회 2024 조직공학과 재생의학 Vol.21 No.1

        Background: Collagen is a key component of connective tissue and has been frequently used in the fabrication of medical devices for tissue regeneration. Human-originated collagen is particularly appealing due to its low immune response as an allograft biomaterial compared to xenografts and its ability to accelerate the regeneration process. Ethically and economically, adipose tissues available from liposuction clinics are a good resource to obtain human collagen. However, studies are still scarce on the extraction and characterization of human collagen, which originates from adipose tissue. The aim of this study is to establish a novel and simple method to extract collagen from human adipose tissue, characterize the collagen, and compare it with commercial-grade porcine collagen for tissue engineering applications. Methods: We developed a method to extract the collagen from human adipose tissue under quasi-Good Manufacturing Practice (GMP) conditions, including freezing the tissue, blood removal, and ethanol-based purification. Various techniques, including protein quantification, decellularization assessment, SDS-PAGE, FTIR, and CD spectroscopy analysis, were used for characterization. Amino acid composition was compared with commercial collagen. Biocompatibility and cell proliferation tests were performed, and in vitro tests using collagen sponge scaffolds were conducted with statistical analysis. Results: Our results showed that this human adipose-derived collagen was equivalent in quality to commercially available porcine collagen. In vitro testing demonstrated high cell attachment and the promotion of cell proliferation. Conclusion: In conclusion, we developed a simple and novel method to extract and characterize collagen and extracellular matrix from human adipose tissue, offering a potential alternative to animal-derived collagen for xeno-free tissue engineering applications. Background: Collagen is a key component of connective tissue and has been frequently used in the fabrication of medical devices for tissue regeneration. Human-originated collagen is particularly appealing due to its low immune response as an allograft biomaterial compared to xenografts and its ability to accelerate the regeneration process. Ethically and economically, adipose tissues available from liposuction clinics are a good resource to obtain human collagen. However, studies are still scarce on the extraction and characterization of human collagen, which originates from adipose tissue. The aim of this study is to establish a novel and simple method to extract collagen from human adipose tissue, characterize the collagen, and compare it with commercial-grade porcine collagen for tissue engineering applications. Methods: We developed a method to extract the collagen from human adipose tissue under quasi-Good Manufacturing Practice (GMP) conditions, including freezing the tissue, blood removal, and ethanol-based purification. Various techniques, including protein quantification, decellularization assessment, SDS-PAGE, FTIR, and CD spectroscopy analysis, were used for characterization. Amino acid composition was compared with commercial collagen. Biocompatibility and cell proliferation tests were performed, and in vitro tests using collagen sponge scaffolds were conducted with statistical analysis. Results: Our results showed that this human adipose-derived collagen was equivalent in quality to commercially available porcine collagen. In vitro testing demonstrated high cell attachment and the promotion of cell proliferation. Conclusion: In conclusion, we developed a simple and novel method to extract and characterize collagen and extracellular matrix from human adipose tissue, offering a potential alternative to animal-derived collagen for xeno-free tissue engineering applications.

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