報(bào)告題目：Electron Transfer in Peptides: Experimental Evidence and Theoretical Insights

報(bào) 告 人：Jingxian Yu, John Horsley (The University of Adelaide)

報(bào)告時(shí)間：2015年10月13日上午9：30

報(bào)告地點(diǎn)：化學(xué)樓二樓一號(hào)會(huì)議室

報(bào)告人簡(jiǎn)介：

     Dr Jingxian Yu completed his BEng, MSc and DSc (electrochemistry) degrees in China and his PhD (nanotechnology) in Australia. Upon the completion of his PhD program he moved to the University of Cambridge, UK as a Roger Pysden Research Fellow and later the University of Nottingham, UK as a postdoctoral research fellow. He returned to Australia in 2009 to take up an ARC Australian Postdoctoral Fellowship (APD) at the University of Adelaide. Presently he is an ARC Centre of Excellence for Nanoscale BioPhotonics (CNBP) senior researcher at the same university. He has a specific interest in electron transfer in peptides using combined electrochemical and computational techniques, and a growing interest in the biological applications of nanomaterials. He is a recipient of a number of awards, including the CASS Foundation Award,Roger Pysden Memorial Fellowship, Ian Potter Foundation Award, Flinders UniversityOverseas Travelling Fellowship and AMY Forwood Travelling Award.

Dr John Horsley completed his BSc (Hons) at Flinders University, before undertaking a PhD at the University of Adelaide in 2011, working exclusively on electron transfer in peptides. He is currently employed by the Centre of Excellence for Nanoscale BioPhotonics (CNBP) at the University of Adelaide, researching means todetect protein/protein interaction to further our understanding of fundamental biological processes at the molecular level.

報(bào)告簡(jiǎn)介：

    Natural proteins have evolved to promote electron transfer in many biological processes. However, their complex conformational nature inhibits a thorough investigation, so in order to study electron transfer in proteins, simple peptide models containing redox active moieties present as ideal candidates. Here, a series of peptides constrained into either helical or β-strand onformations have been synthesized for electrochemical analysis. The effect of backbone igidity imparted by a side-bridge constraint was revealed, which was shown to restrict the necessary torsional motion that leads to facile intramolecular electron transfer along the peptide backbone. High level calculations were used to support the electrochemical observations on all significant findings. This provides a new approach for fine tuning the electronic properties of peptides through manipulation of their structural and chemical characteristics in order to progress the field of molecular electronics.