<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kapp, Tobias G.</style></author><author><style face="normal" font="default" size="100%">Di Leva, Francesco Saverio</style></author><author><style face="normal" font="default" size="100%">Notni, Johannes</style></author><author><style face="normal" font="default" size="100%">Raeder, Andreas F. B.</style></author><author><style face="normal" font="default" size="100%">Fottner, Maximilian</style></author><author><style face="normal" font="default" size="100%">Reichart, Florian</style></author><author><style face="normal" font="default" size="100%">Reich, Dominik</style></author><author><style face="normal" font="default" size="100%">Wurzer, Alexander</style></author><author><style face="normal" font="default" size="100%">Steiger, Katja</style></author><author><style face="normal" font="default" size="100%">Novellino, Ettore</style></author><author><style face="normal" font="default" size="100%">Marelli, Udaya Kiran</style></author><author><style face="normal" font="default" size="100%">Wester, Hans-Juergen</style></author><author><style face="normal" font="default" size="100%">Marinelli, Luciana</style></author><author><style face="normal" font="default" size="100%">Kessler, Horst</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">N-Methylation of isoDGR peptides: discovery of a selective alpha 5 beta 1-integrin ligand as a potent tumor imaging agent</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Medicinal Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">61</style></volume><pages><style face="normal" font="default" size="100%">2490-2499</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">6.259</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Meena, Chhuttan L.</style></author><author><style face="normal" font="default" size="100%">Singh, Dharmendra</style></author><author><style face="normal" font="default" size="100%">Weinmueller, Michael</style></author><author><style face="normal" font="default" size="100%">Reichart, Florian</style></author><author><style face="normal" font="default" size="100%">Dangi, Abha</style></author><author><style face="normal" font="default" size="100%">Marelli, Udaya Kiran</style></author><author><style face="normal" font="default" size="100%">Zahler, Stefan</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Novel cilengitide-based cyclic RGD peptides as alpha nu beta(3) integrin inhibitors</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anticancer drugs</style></keyword><keyword><style  face="normal" font="default" size="100%">Cilengitide</style></keyword><keyword><style  face="normal" font="default" size="100%">Integrins</style></keyword><keyword><style  face="normal" font="default" size="100%">RGD cyclicpeptides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">127039</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In this letter, we report a series of five new RGD-containing cyclic peptides as potent inhibitors to alpha nu beta(3) integrin protein. We have incorporated various unnatural lipophilic amino acids into the cyclic RGD framework of cilengitide, which is selective for alpha nu beta(3) integrin. All the newly synthesized cyclic peptides were evaluated in vitro solid phase binding assay and investigated for their binding behaviour towards integrin subtypes. All the cyclic peptides were synthesized in excellent yield following solution-phase coupling strategy. The cyclic RGD peptides 1a-e exhibited IC50 of 9.9, 5.5, 72, 11 and 3.3 nM, respectively, towards a alpha nu beta(3) integrin protein. This finding offers further opportunities for the introduction unusual amino acids into the cyclic peptide framework of cilengitide.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;2.572&lt;/p&gt;
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