返回主页 Sun

开放交流

联系我们

联 系 人:兰老师
电 话:010-64412084
传 真:010-64427698
电子邮件:lanjl@mail.buct.edu.cn
邮 编:100029
您当前的位置: 首页» 开放交流» 学术报告» Boronic Acids: Recognition, Sensing and Assembly

Boronic Acids: Recognition, Sensing and Assembly

责编: | 发布日期:2016-12-16| 阅读次数:
 类别    学术报告
发布单位    理学院
报告(活动)名称    Boronic Acids: Recognition, Sensing and Assembly  
报告(活动)时间    2016/12/19 9:30:22 至2016/12/19 10:30:30  
报告(活动)地点    图书馆中心会议室
报告(活动)人数    100
报名时间     2016/12/13 12:39:00 至2016/12/19 9:39:01
报告(活动)内容    The ability to monitor analytes within physiological, environmental and industrial scenarios is of prime importance. Since recognition events occur on a molecular level, gathering and processing the information poses a fundamental challenge. Therefore robust chemical molecular sensors “chemosensors” with the capacity to detect chosen molecules selectively and signal this presence continue to attract considerable attention. Real-time monitoring of saccharides is of particular interest, such as D-glucose in blood. Towards that end the covalent coupling interaction between boronic acids and saccharides has been exploited with some success to monitor the presence of such saccharides. The boronic acid based Lewis acid-base interaction is also suitable for the capture and recognition of anions. Anions are involved in fundamental processes in all living things. Our aim is to mimic nature’s level of sophistication in designing and producing chemosensors capable of determining the concentration of a target species such as: saccharides, glycated proteins, anions and reactive oxygen/nitrogen species (ROS/RNS) in any medium. As well as sensors for saccharides, anions and ROS/RNS the presentation will cover the use of boronic acid based receptors for the analysis of protein glycation. Protein glycation is an important biomarker for age-related disorders such as diabetes and Alzheimer’s disease. This process whereby reducing saccharides react with amino groups of proteins ultimately leads to the formation of complex and stable advanced glycation endproducts (AGEs). Glycation compromises proteins throughout the body resulting in many diabetes related complications (e.g., nerve damage, heart attack, and blindness). Glycated proteins and their resulting AGE products are also key elements in the pathology of Alzheimer’s Disease (AD). 报告人简介 Tony D James: Professor at the University of Bath and Fellow of the Royal Society of Chemistry. He obtained his: BSc 1986 (University of East Anglia), PhD 1991 (University of Victoria), and was a Postdoctoral Research Fellow 1991-95 (with Seiji. Shinkai in Japan). He was a Royal Society Research Fellow from 1995 to 2000 (University of Birmingham). In 2013 he was recognized for his role in developing networks with Japan by the award of a Daiwa-Adrian Prize and in 2015 he received the Inaugural CASE Prize for establishing and developing networks with China. His research interests include many aspects of Supramolecular chemistry, including: molecular recognition, molecular self-assembly and sensor design.