http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 주제어 : Fibrillogenesis (검색결과 5 건)
- 무료
- 기관 내 무료
- 유료
-
Merlin Jayalal, L.P. The Basic Science Institute Chosun University 2012 조선자연과학논문집 Vol.5 No.2
Polymerization of monomeric amyloid-${\beta}$ peptides ($A{\beta}$) into soluble oligomers and insoluble fibrils is one of the major pathways triggering the pathogenesis of Alzheimer's disease (AD). Using small molecules to prevent the polymerization of $A{\beta}$ peptides can, therefore, be an effective therapeutic strategy for AD. In this study, we investigated the effects of mono- and bi-flavonoids on $A{\beta}42$ toxicity and fibrillogenesis and found that the bi-flavonoid, taiwaniaflavone (TF) effectively and specifically inhibits $A{\beta}$ toxicity and fibrillogenesis. Compared to TF, the mono-flavonoid apigenin (AP) is less effective and less specific. Our data showed that differential effects of the mono- and bi-flavonoids on $A{\beta}$ fibrillogenesis correlate with their varying cytoprotective efficacies. We also found that other bi-flavonoids, namely 2',8"-biapigenin, amentoflavone, and sumaflavone, can also effectively inhibit $A{\beta}$ toxicity and fibrillogenesis, implying that the participation of two mono-flavonoids in a single bi-flavonoid molecule enhanced their activity. Bi-flavonoids, while strongly inhibited $A{\beta}$ fibrillogenesis, accumulated nontoxic $A{\beta}$ oligomeric structures, suggesting that these are off-pathway-oligomers. Moreover, TF abrogated the toxicity of preformed $A{\beta}$ oligomers and fibrils, indicating that TF and other bi-flavonoids may also reduce the toxicity of toxic $A{\beta}$ species. Altogether, our data clearly show that bi-flavonoids, possibly due to the possession of two $A{\beta}$ binders separated by an appropriate size linker, are likely to be promising therapeutics to suppress $A{\beta}$ toxicity.
-
Md. Anisuzzaman Chowdhury,고해주,이환,Md. Aminul Haque,박일선,이동성,우은란 대한약학회 2017 Archives of Pharmacal Research Vol.40 No.3
Previous phytochemical investigations of Akebiae compound 1 and the inhibitory effects of components fromAkebiae Caulis on Ab42 fibrillogenesis. Caulis resulted in the isolation of triterpenes, triterpeneglycosides, phenylethanoid glycosides and megastigmaneglycoside. Amyloid beta (Ab), the main component of thesenile plaques detected in Alzheimer’s disease, induces celldeath. However, only a limited number of studies haveaddressed the biological and pharmacological effects ofAkebiae Caulis. In particular, the inhibitory activity ofAkebiae Caulis against Ab42 fibrillogenesis remainsunclear. Herein, a new triterpene glycoside, akequintoside F(1), along with nine known compounds pulsatilla saponin A(2), collinsonidin (3), akebonic acid (4), hederagenin (5),1-(30,40-dihydroxycinnamoyl) cyclopentane-2,3-diol (6),asperosaponin C (7), leontoside A (8), quinatic acid (9), andquinatoside A (10) were isolated from Akebiae Caulis usingrepeated column chromatography with silica gel, LiChroprepRP-18, and MCI gel. The chemical structures ofcompounds 1–10 were illustrated based on 1D and 2D NMRspectroscopy, including 1H-1H COSY, HSQC, HMBC andNOESY spectroscopic analyses. Compound 1 a novelcompound and known compounds 6 and 7 were isolated forthe first time from this plant. Among these compounds, 1, 3,4, 5 and 7 displayed significant inhibitory effects on Ab42induced fibrillogenesis. We present the first report of new
-
Ground type-I collagen—a focused study on its fibrillogenesis behavior and bioactivity in vitro
Yuling Xu,Lei Dai,Ke Li,Jialin Liu,Haibo Wang,Lang He,Chengzhi Xu,Benmei Wei,Juntao Zhang 한국고분자학회 2023 Macromolecular Research Vol.31 No.1
Take bovine tendon type-I collagen as the raw material, we pretreated it by freezing and then grinding the macromolecule at a low temperature (4–10 °C). Effects of the grinding process on the molecular structure, water solubility, fibrillogenesis behavior in vitro and biological activity of collagen were systematically prospected. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) results revealed that the collagen had typical structural characteristics of type-I collagen; moreover, grinding treatment gave rise to partially degraded collagen molecules which took on continuous bands with lower molecular weights different from α1 and α2. More strikingly, the degradation degree positively corresponded to the grinding duration. Circular dichroism (CD) analysis manifested that with extended grinding, intensities of both the positive and negative peaks for collagen samples shrunk. Interestingly, grinding also contributed to improved water solubility of collagen. The water solubility of the sample ground for 20 min (COL20) was 1.91 mg/mL, which is about 6 times higher than that of the natural collagen sample (0.28 mg/mL). Amid the study concerning the fibrillogenesis behavior, turbidity and rheological data collaboratively demonstrated that with prolonged grinding time, the assembly rate and degree of the sample plunged. Assembled gel from the ground collagen with finer fibrils was also observed in scanning electron microscope (SEM), which further embraced the conclusion aforementioned in fibrillogenesis kinetics. Cell experiments corroborated that the grinding process can be harnessed to manipulate the cell proliferation promoting ability of collagen. Simultaneously, further dissection of COL20 with the best biological activity clarified that the water-soluble part and water-insoluble part of COL20 had distinct aptitudes as to promoting cell proliferation as well as inhibiting the growth of liver cancer cells.
-
-
Effect of UV on Stability of Collagen with Consideration of Hydratation and Fibrillogenesis
Jian-Yu Xing,Bo Bai,Wen-Jiao Xue,Ming-Yan Yang 한국식품과학회 2013 Food Science and Biotechnology Vol.22 No.5
Collagen is an abundant extracellular matrix protein that is widely used in the biomaterial, food, and medical fields. Most extracted collagen is soluble in acids and assembles into fibrils under neutral pH conditions. In order to study the effect of UV irradiation on the stability of collagen with consideration of hydratation and fibrillogenesis,UV irradiation of collagen under acid and neutral pH conditions was investigated using electrophoresis, turbidity analysis, and Fourier transform infrared spectroscopy. The relationship between the collagen structure and sensitivity to UV radiation was assessed by studying the effect of UV on collagen under different pH conditions. Results showed that structural changes in collagen caused by UV depend on the degree of hydratation. Soluble collagen completely loses fibrillogeneic ability after exposure to UV for 40 min. Fibrillogenesis of collagen can relieve the UV effect to some degree.
eArticle연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
