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纳米金放大SPR技术检测前列腺癌肿瘤标志物free PSA
  • ISSN号:1004-5929
  • 期刊名称:《光散射学报》
  • 时间:0
  • 分类:O614.121[理学—无机化学;理学—化学] Q517[生物学—生物化学]
  • 作者机构:[1]Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education of China, School of Chemistry and ChemicalEngineering, Hunan University of Science and Technology, Xiangtan 411201, China, [2]Institute of Surface Analysis and Biosensing, College of Chemistry and Chemical Engineering, Central South University, Changsha 410083, China, [3]Key Laboratory of Resources Chemistry of Nonferrous Metals, Ministry of Education, Central South University, Changsha 410083, China
  • 相关基金:This work was supported by grants from the Postdoctoral Science Foundation of China, the National Natural Science Foundation of China (No. 20773165), the Scientific Research Fund of Hunan Provincial, the Science Foundation of Hunan Province, the Program for New Century Excellent Talents in University (No. NCET-07-0865), and the Post- doctoral Science Foundation of Central South University (No. P20-MD001824-01).
中文摘要:

它是众所周知的聚集淀粉 --Cu2+ 导致的肽(A) 与孵化时间,答案 pH,和温度有关。在这个工作, A142 的聚集在不同孵化时间和温度面对在酸的条件下面的 Cu2+ 被学习(例如 25 和 37 ?????  ?? 匠吗??

英文摘要:

It is well known that the aggregation of amyloid-β peptide (Aβ) induced by Cu^2+ is related to incubation time, solu-tion pH, and temperature. In this work, the aggregation of Aβ1-42 in the presence of Cu^2+ under acidic conditions was studied at different incubation time and temperature (e.g. 25 and 37℃). Incubation temperature, pH, and the presence of Cu^2+ in Aβ solution were confirmed to alter the morphology of aggregation (fibrils or amorphous aggregates), and the morphology is pivotal for Aβ neuro-toxicity and AIzheimer disease (AD) development. The results of atomic force microscopy (AFM) indicated that the formation of Aβ fibrous morphology is preferred at lower pH, but Cu^2+ induced the formation of amorphous aggregates. The aggregation rate of Aβ was increased with the elevation of temperature. These results were further confirmed by fluorescence spectroscopy and circular di-chroism spectroscopy and it was found that the formation of β-sheet structure was inhibited by Cu^2+ binding to Aβ. The result was consistent with AFM observation and the fibrillation process was restrained. We believe that the local charge state in hydrophilic domain of Aβ may play a dom-inant role in the aggregate morphology due to the strong steric hindrance. This research will be valuable for under-standing of Aβ toxicity in AD.

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期刊信息
  • 《光散射学报》
  • 中国科技核心期刊
  • 主管单位:四川省科学技术协会
  • 主办单位:中国物理学会光散射专业委员会 四川省物理学会
  • 主编:李灿
  • 地址:四川省成都四川大学物理科学与技术学院
  • 邮编:610064
  • 邮箱:
  • 电话:028-85418067
  • 国际标准刊号:ISSN:1004-5929
  • 国内统一刊号:ISSN:51-1395/O4
  • 邮发代号:
  • 获奖情况:
  • 曾为Caj-cd规范获奖期刊
  • 国内外数据库收录:
  • 中国中国科技核心期刊,中国北大核心期刊(2008版),中国北大核心期刊(2011版),中国北大核心期刊(2014版)
  • 被引量:2405