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发布时间:2019-08-22 14:08:00
澳大利亚科学与工程院院士Ronald J Quinn教授1970年在新南威尔士大学获博士学位,1982年加入格里菲斯大学,1994年被任命为教授,是Eskitis细胞与分子治疗研究所(现格里菲斯药物研究所)的创始人和前所长。
Quinn教授创办了澳洲最大的天然样本库Nature Bank,现存超过7万种来自澳大利亚、中国和巴布亚新几内亚等地的植物、海洋生物及微生物样本,以及大量提取物组分和纯化合物样品,为科研机构和企业提供了丰富的资源;他还是化合物库Compounds Australia的创始人之一,现存样品数超过60万,已成为澳大利亚的化合物存储于管理中心。Quinn教授多年在国际高水平杂志上共发表论文近300篇,参与编写学术专著15部,专利10余项,作为项目负责人获NGC基金资助项目、国际工业合作项目、国际竞争性基金等多类资助项目数10项,总和约1亿5千万澳元。
Quinn教授的研究兴趣聚焦于利用小分子为探针,阐明生命体系的相互作用,研究工作涉及活性天然产物和生物亲和质谱技术鉴定蛋白质-配体的复合物等。具体包括基于分子靶点的高通量生物活性筛选、活性天然化合物的分离和结构鉴定、受体配体和蛋白酶抑制剂的设计与合成,认识药物发现中基于天然产物的生物合成酶辨识可能治疗靶点的途径等。
2010年获澳大利亚爵级司令勋章;2013年获McCullough Robertson LSQ工业杰出成就奖;2014年上海药物所“一三五”诊断评估国际专家;2009、2015年格里菲斯大学校长“杰出研究奖”研究带头人;2016年格里菲斯大学校长“杰出研究奖”终身研究带头人;2016年Paul J Scheuer奖获得者;2018年入选中国科学院国际人才计划(PIFI)国际杰出学者;2018年华东理工大学名誉教授
Decoding the Language of Nature and Fragment-based Mass Spectrometry
Ronald J. Quinn
Griffith Institute for Drug Discovery, Griffith University, Australia,E-mail: r.quinn@griffith.edu.au
Currently, there is no established technique that allows the function of a compound produced by nature to be predicted by looking at its chemical structure. One of chemistry’s grand challenges: to find a function for every metabolite.
The profound and specific biological activity of natural products coupled with their immediately recognizable structures suggests a code within these structures that we are not as yet aware of. The long-standing challenge is to be able to decode the functional information entangled in the structures of these metabolites, selected over millions of years by continuous evolution.
We explore the opportunity for Artificial Intelligence to provide rationale interrogation of metabolites.
Native Mass Spectrometry using a Magnetic Resonance Mass Spectrometer (MRMS) can detect protein in its native folded state and can detect and distinguish noncovalent and covalent protein-ligand complexes.
We have harnessed the chemical diversity of natural products for fragment-based drug screening. We have reported 96 low molecular weight natural products identified as binding partners of 32 putative malarial targets. Seventy-nine (79) fragments have direct growth inhibition on Plasmodium falciparum at concentrations that are promising for development of fragment hits against these protein targets. This adds a fragment library to the published HTS active libraries in the public domain.
Subsequently, we have identified 26 low molecular weight natural products that bind to 9 proteins from Mycobacterium tuberculosis.
We have developed a fast target ID strategy following a cellular assay against mycobacterium tuberculosis using native Mass spectrometry.