Kyushu University · 생화학·유전·분자생물학
Noriho Kamiya 교수의 연구실은 단백질 공학과 생체분자 라벨링 기술을 중심으로, 마이크로벌 트랜스글루타민산효소(MTG)를 활용한 고특이적 단백질 접합 기반의 생물학적 분자 조립 기술을 개발하고 있습니다. 특히 N-터미널 글리신을 이용한 타겟 단백질의 정밀한 유도체화 및 DNA-단백질 접합을 통해 단백질 기반 나노소재 및 세포 레지스트리 시스템을 구축하고 있으며, 이는 의약품 개발 및 세포 치료에 응용될 수 있습니다. 또한, 효소 기반의 산화적 접합 반응을 이용한 생체 적합성 수화제 개발도 진행 중입니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
Here, we report the N-terminal glycine (Gly) residue of a target protein can be a candidate primary amine for site-specific protein conjugation catalyzed by microbial transglutaminase (MTG) from Streptomyces mobaraensis. Gly5-enhanced green fluorescent protein (EGFP) (EGFP with five additional Gly residues at its N-terminus) was cross-linked with Myc-dihydrofolate reductase (DHFR) (DHFR with the myc epitope sequence at its N-terminus) to yield DHFR-EGFP heterodimers. The reactivities of addition
Abstract Enantioselective esterification of menthol with fatty acids using a surfactant‐coated lipase was carried out in organic media. The surfactant‐coated lipase originating from Candida cylindracea appeared to be highly enantioselective and good biocatalyst for the resolution of racemic menthol. The enzymatic activity of the lipase in organic media was significantly increased by a coating with a nonionic surfactant. The reaction rate of the coated lipase was more than 100 times that of the p
DNA was site-specifically conjugated to a substrate peptide of microbial transglutaminase fused to the N- or C-terminus of target proteins without the loss of the proteins' functions of interest.
Horseradish peroxidase-mediated oxidative cross-linking of a thiolated poly(ethylene glycol) is promoted in the absence of exogenous hydrogen peroxide, by adding a small amount of a phenolic compound under physiological conditions. The prepared hydrogel can encapsulate and release living mammalian cells.
