题目：Resolving antimicrobial and amyloid peptides in membranes
主持人：北大医学部神经科学研究所崔德华教授,（电话：010-8280-2920）
报告时间：2010年10月22日上午10点
报告地点：北大医学部国合处会议室（详见地图附件）
联系人：北医国合处李晓佳Tel: 86-10-82802236
报告摘要：The results of solid-state NMR studies aimed at determining the orientation and location of antimicrobial peptides obtained from Australian tree frogs and amyloid peptides in phospholipid membranes will be discussed. The detailed structure of these peptides in membranes is difficult to determine as they disrupt the phospholipid bilayer. Solid-state NMR techniques are being used to determine the conformation and mobility of these pore-forming peptides in order to understand the mechanisms by which they exert their biological effect that leads to the disruption of biological membranes. Both static and magic angle spinning techniques have been applied to antimicrobial peptides in a range of model membranes, which reveal that the peptide activity is strongly dependent on the lipid composition of the bilayer and correlate with the ivity for bacterial membranes. Similarly, the membrane interactions and structural changes of Aβ(1-42) and Aβ(1-40) from Alzheimer’s disease are dependent on the presence of cholesterol and metal ions, which have been implicated in the disease. The data from both the amyloid and antimicrobial peptides reveal the importance of using appropriate membranes systems for studying membrane-active peptides.
报告人简介
Professor , School of Chemistry, The University of Melbourne
Associate Professor and Reader, University of Melbourne, 1996-2005
Professor, University of Melbourne, 2005-
Associate Dean International, Faculty of Science, University of Melbourne, 2009-
Head, School of Chemistry, University of Melbourne, 2010-
Areas of Interest
Physical Chemistry
Biological and Medicinal Chemistry
Spectroscopy and Molecular Characterisation
RResearch:NMR spectroscopy, complemented by a range of biophysical techniques, is being used to determine the structure and dynamics of membrane polypeptides to determine their mechanism of activity.
Currently our main focus is the structure and interactions of amyloid peptides from Alzheimer’s disease, pore-forming toxins and antibiotic peptides in model biological membranes.
The results of our research provide insights the biophysical chemistry of membrane-active peptides and proteins relevant to Alzheimer’s disease states and their possible treatments.
