Exploració per autor "Kessler, H."
Ara es mostren els items 1-7 de 7
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Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch
Frank, A.O.; Otto, E.; Mas Moruno, Carlos; Schiller, H.; Marinelli, L.; Cosconati, S.; Bochen, A.; Vossmeyer, D.; Zahn, G.; Stragies, R.; Novellino, E.; Kessler, H. (2010)
Article
Accés restringit per política de l'editorialThumbnail image of graphical abstract The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a ... -
Cyclic azapeptide integrin ligand synthesis and biological activity
Spiegel, J.; Mas Moruno, Carlos; Kessler, H.; Lubell, W.D. (2012)
Article
Accés restringit per política de l'editorialAza-peptides are obtained by replacement of the α-C-atom of one or more amino acids by a nitrogen atom in a peptide sequence. Introduction of aza-residues into peptide sequences may result in unique structural and ... -
Increasing avß3 selectivity of the anti-angiogenic drug cilengitide by N-methylation
Mas Moruno, Carlos; Beck, J.G.; Doedens, L.; Frank, A.O.; Marinelli, L.; Cosconati, S.; Novellino, E.; Kessler, H. (2011)
Article
Accés restringit per política de l'editorialThumbnail image of graphical abstract A subtle change: Structural changes upon amide bond methylation improve the selectivity of the anti-angiogenic drug Cilengitide, which after N-methylation at distinct positions ... -
Introducing lasso peptides as molecular scaffolds for drug design: Engineering of an integrin antagonist.
Knappe, T.A.; Manzenrieder, F.; Mas Moruno, Carlos; Linne, U.; Sasse, F.; Kessler, H.; Xie, X.; Marahiel, M.A. (2011)
Article
Accés restringit per política de l'editorialThumbnail image of graphical abstract Tightening the noose: Lasso peptides are a class of stable bacterial peptides with unique characteristics that encourage their application in drug design. Epitope grafting of the ... -
Polymer-free immobilization of a cyclic RGD peptide on a nitinol stent promotes integrin-dependent endothelial coverage of strut surfaces
Joner, M.; Cheng, Q.; Schönhofer-Merl, S.; Lopez, M.; Neubauer, S.; Mas Moruno, Carlos; Laufer, B.; Kolodgie, F.D.; Kessler, H.; Virmani, R. (2012)
Article
Accés restringit per política de l'editorial
Realitzat a/amb: Technische Universität München / CVPath InstituteThis study examined the utility of a stabilized cyclic RGD peptide chemically modified to selectively bind to titanium-oxide for enhanced biocompatibility of self-expanding nitinol stents. Endothelial cells express integrin ... -
Solid-phase-assisted synthesis of targeting peptide-PEG-oligo(ethane amino)amides for receptor-mediated gene delivery
Martin, I.; Dohmen, C.; Mas Moruno, Carlos; Troiber, C.; Kos, P.; Schaffert, D.; Lächelt, U.; Teixidó, M.; Günther, M.; Kessler, H.; Giralt, E.; Wagner, E. (2012)
Article
Accés obert
Realitzat a/amb: Technische Universität MünchenIn the forthcoming era of cancer gene therapy, efforts will be devoted to the development of new efficient and non-toxic gene delivery vectors. In this regard, the use of Fmoc/Boc-protected oligo(ethane amino)acids as ... -
The impact of amino acid side chain mutations in conformational design of peptides and proteins
Laufer, B.; Frank, A.O.; Chatterjee, J.; Neubauer, T.; Mas Moruno, Carlos; Kummerlöwe, G.; Kessler, H. (2010)
Article
Accés restringit per política de l'editorial
Realitzat a/amb: Technische Universität MünchenLocal energetic effects of amino acid replacements are often considered to have only a moderate influence on the backbone conformation of proteins or peptides. As these effects are difficult to determine experimentally, ...