Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

Nicola McMillan; Louise V. Smith; Jesus M. de la Fuente; Alexis D. C. Parenty; Nikolaj Gadegaard; Andrew R. Pitt; Katrina Thomson; Cameron MacKenzie; Sharon M. Kelly; Leroy Cronin

doi:10.1039/B702575K

Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification†

Nicola McMillan,^a Louise V. Smith,^a Jesus M. de la Fuente,^b Alexis D. C. Parenty,^a Nikolaj Gadegaard,^c Andrew R. Pitt,^d Katrina Thomson,^d Cameron MacKenzie,^a Sharon M. Kelly^d and Leroy Cronin*^a

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* Corresponding authors

^a WestCHEM, Department of Chemistry, The University of Glasgow, University Avenue, Glasgow, UK
E-mail: L.Cronin@chem.gla.ac.uk
Fax: +44-141-330-4888
Tel: +44-141-330-6650

^b Instituto de Nanociencia de Aragon, Universidad de Zaragoza. C/ Pedro Cerbuna 12, Zaragoza 50009, Spain

^c Department of Electronics and Electrical Engineering, University of Glasgow, Glasgow, UK

^d Department of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, Joseph Black Building, University of Glasgow, Glasgow, UK

Abstract

N-Heterocyclic cations are incorporated into proteins using 5-(2-bromoethyl)phenanthridinium bromide, which selectively reacts with either cysteine or lysine residues, resulting in ethylphenanthridinium (Phen) or highly stable cyclised dihydro-imidazo-phenanthridinium (DIP) adducts respectively; these modifications have been found to manipulate the observed structure of lysozyme and bovine serum albumin by AFM.

Chemical Communications

Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification†

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Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

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