检索结果-南通市图书馆

Graphene quantum dots rescue protein dysregulation of pancreatic β-cells exposed to human islet amyloid polypeptide

Nano Research 2019年第11期12卷 2827-2834页

作者： Ava Faridi Yunxiang Sun Monika Mortimer Ritchlynn R.Aranha aparna nandakumar Yuhuan Li Ibrahim Javed Aleksandr Kakinen Qingqing Fan Anthony W.Purcell Thomas P.Davis Feng Ding Pouya Faridi Pu Chun Ke ARC Centre of Excellence in Convergent Bio-Nano Science and Technology Monash Institute of Pharmaceutical SciencesMonash University381 Royal ParadeParkvilleVIC3052Australia Department of Physics Ningbo UniversityNingbo315211China Department of Physics and Astronomy Clemson UniversityClemsonSC29634USA Institute of Environmental and Health Sciences College of Quality and Safety EngineeringChina Jiliang UniversityHangzhou310018China Infection and Immunity Program&Department of Biochemistry and Molecular Biology Biomedicine Discovery InstituteMonash UniversityClaytonVictoria3800Australia Australian Institute for Bioengineering and Nanotechnology The University of QueenslandBrisbaneQld4072Australia

The amyloid aggregation of peptides and proteins is a hallmark of neurological disorders and type 2 *** islet amyloid polypeptide(IAPP),co-secreted with insulin by pancreaticβ-cells,plays dual roles in both glycemic control and the pathology of type 2 *** IAPP can activate the NLRP3 inflammasome and modulate cellular autophagy,apoptosis and extracellular matrix metabolism,no data is available concerning intracellular protein expression upon exposure to the *** surprisingly,how intracellular protein expression is modulated by nanoparticle inhibitors of protein aggregation remains entirely *** this study,we first examined the changing proteomes ofβTC6,a pancreaticβ-cell line,upon exposure to monomeric,oligomeric and fibrillar IAPP,and detailed cellular protein expression rescued by graphene quantum dots(GQDs),an IAPP *** found that 29 proteins were significantly dysregulated by the IAPP species,while majority of these proteins were nucleotide-binding ***,our liquid chromatography tandem-mass spectrometry,fluorescence quenching,helium ion microscopy,cytotoxicity and discreet molecular dynamics simulations data revealed a remarkable capacity of GQDs in regulating aberrant protein expression through H-bonding and hydrophobic interactions,pointing to nanomedicine as a new frontier against human amyloid diseases.

关键词： islet amyloid polypeptide(IAPP) oligomer amyloid protein expression graphene quantum dot

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：