@article {44597,
	title = {N-Methylation of isoDGR peptides: discovery of a selective alpha 5 beta 1-integrin ligand as a potent tumor imaging agent},
	journal = {Journal of Medicinal Chemistry},
	volume = {61},
	year = {2018},
	month = {MAR},
	pages = {2490-2499},
	type = {Article},
	abstract = {<p>Specific targeting of the integrin subtype alpha 5 beta 1 possesses high potential in cancer diagnosis and therapy. Through sequential N-methylation, we successfully converted the biselective alpha 5 beta 1/alpha v beta 6 peptide c(phg-isoDGR-k) into a potent peptidic RGD binding aSfil subtype selective ligand c(phg-isoDGR-(NMe)k). Nuclear magnetic resonance spectroscopy and molecular modeling clarified the molecular basis of its improved selectivity profile. To demonstrate its potential in vivo, c(phg-isoDGR-(NMe)k) was trimerized with the chelator TRAP and used as a positron-emission tomography tracer for monitoring alpha 5 beta 1 integrin expression in a M21 mouse xenograft.</p>},
	issn = {0022-2623},
	doi = {10.1021/acs.jmedchem.7b01752},
	author = {Kapp, Tobias G. and Di Leva, Francesco Saverio and Notni, Johannes and Raeder, Andreas F. B. and Fottner, Maximilian and Reichart, Florian and Reich, Dominik and Wurzer, Alexander and Steiger, Katja and Novellino, Ettore and Marelli, Udaya Kiran and Wester, Hans-Juergen and Marinelli, Luciana and Kessler, Horst}
}
