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- 저자 : Yunfeng Ma (검색결과 2 건)
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LI HOU,Yunfeng Niu,Yan Wang,YANG JIANG,Rongna Chen,Tianran Ma,FAMING GAO 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2016 NANO Vol.11 No.6
Here, we present a simple and novel method based on using insulin amyloid fibrils (INSAFs) as sacrificial templates for the construction of Pt–Pd nanoparticle chains (Pt–PdNPCs) under mild conditions. By incubating INSAFs in metal salt solution and then reduction, Pt–Pd nanoparticles with an uniform particle size of around 2.5 nm nucleated and grew along the axial direction of INSAFs, and thus formed a long chain structure with length up to several micrometers. The as-prepared Pt–PdNPCs exhibit an improved catalytic activity for lowtemperature CO and methanol oxidation and possess greater CO tolerance compared with the commercial Pt/C catalyst, which makes them promising for a variety of possible catalytic applications.
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Fengling Luo,Yubin Wang,Xiaoming Sun,Qilong Wang,Yunfeng Ma,Qin Pan,Xiao-Lian Zhang 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
Tuberculosis (TB) caused by Mycobacterium tuberculosis (M.tb) remains a major global health problem. Human ficolin2 (L-ficolin/P35) is a recently identified lectin complement pathway activator present in normal plasma associated with infectious diseases, however, little is known about the roles and mechanisms of ficolin2 during M.tb infection.We describe in this study for the first time L-ficolin expression levels in tuberculosis (TB) patients. We found that serum levels of ficolin2 of 107 pulmonary TB patients were much lower compared with 107 healthy controls, and recurrence TB patients have even lower levels than onset TB patients. In vitro analysis showed that Ficolin2 bound to virulent M.tb H37Rv strain much stronger than to non-virulent M. bovis BCG and M. smegmatis. Ficolin2/ficolin A bound to the H37Rv surface glycolipid portion and blocked H37Rv infection to human lung A549 cells. We further determined that the extrogenous ficolin2 had remarkable protecting effects against virulent H37Rv strain infections in C57BL/6J mice. FicolinA (ficolin2 like molecule) knockout mice had greatly increased susceptibility to the H37Rv infection. Ficolin2 activated macrophages via phosphorylation of JNK and stimulated IFN-□, IL-17, TNF-□ and nitric oxide (NO) secretions. Ficolin2 also stimulated IFN-□ production of CD8+T cells, but not CD4+T cells. The opsono-phagocytosis was promoted by ficolin2 as well. Our data demonstrate that ficolin2 can defend against virulent M.tb H37Rv infection both in vitro and in vivo mainly via activating macrophage proinflammatory cytokines IFN-□ and NO production and opsonophagocytosis, and its insufficiency is associated with more susceptible infections in human.
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