The fluorinase enzyme as a tool for fluorine-18 incorporation

Published on January 4, 2013

The video describes the background to the origin of the fluorinase enzyme from Streptomyces cattleya, which has the ability to form a C-F bond with inorganic fluoride.

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The presentation describes the isolation and purification of the enzyme and illustrates how it can be used, in a two-enzyme reaction, to prepare [5-18F]-5-fluoro-5-deoxyribose ([18F]-FDR). The sugar [18F]-FDR emerges as an excellent ligand for bioconjugation to clinically significant peptides. Moreover, it holds promise as a new methodology for labelling peptides with the fluorine-18 isotope, for application in clinical imaging by positron emission tomography (PET).

O'Hagan Group | University of St Andrews, UK

Professor David O’Hagan is Head of Organic Chemistry at the University of St Andrews in Scotland. He has studied and worked at the Universities of Glasgow (B. Sc), Southampton (Ph.D), Ohio State and Durham (UK). He moved to St Andrews in 2000. He is interested in organo-fluorine chemistry and biochemistry, and his lab has led the development of enzymatic fluorination and its application as a catalyst for the synthesis of new imaging molecules for positron emission tomography.

Nouchali Bandaranayaka is a Ph.D student in the St Andrews laboratory working with Professor O’Hagan. She is originally from Sri Lanka, and carried out her undergraduate degree in Molecular Biology at the University of Dundee.

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