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Combination of phage display and molecular grafting generates highly specific tumor-targeting miniproteins

Frankenstein′s peptide: The grafting of the binding domain from miniprotein Min-23 into the sunflower trypsin inhibitor (SFTI-I) peptide scaffold (see scheme) preserved its in vitro and in vivo binding specificity and proteolytic stability. The combination of these peptides was shown to be tumor-spe...

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Bibliographische Detailangaben
Hauptverfasser: Zoller, Frederic (VerfasserIn) , Markert, Annette (VerfasserIn) , Zhao, Wenye (VerfasserIn) , Weichert, Wilko (VerfasserIn) , Askoxylakis, Vasileios (VerfasserIn) , Altmann, Annette (VerfasserIn) , Mier, Walter (VerfasserIn) , Haberkorn, Uwe (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: November 13, 2012
In: Angewandte Chemie. International edition
Year: 2012, Jahrgang: 51, Heft: 52, Pages: 13136-13139
ISSN:1521-3773
DOI:10.1002/anie.201203857
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1002/anie.201203857
Verlag, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201203857
Volltext
Verfasserangaben:Frederic Zoller, Annette Markert, Philippe Barthe, Wenye Zhao, Wilko Weichert, Vasileios Askoxylakis, Annette Altmann, Walter Mier, and Uwe Haberkorn
Beschreibung
Zusammenfassung:Frankenstein′s peptide: The grafting of the binding domain from miniprotein Min-23 into the sunflower trypsin inhibitor (SFTI-I) peptide scaffold (see scheme) preserved its in vitro and in vivo binding specificity and proteolytic stability. The combination of these peptides was shown to be tumor-specific with a good binding affinity for delta-like ligand 4 (Dll4) protein. The use of SFTI-I as a peptide scaffold is ideal for hit-to-lead development.
Beschreibung:Gesehen am 23.08.2018
Beschreibung:Online Resource
ISSN:1521-3773
DOI:10.1002/anie.201203857

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