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Combination of Phage Display and Molecular Grafting Generates Highly Specific Tumor‐Targeting Miniproteins
Author(s) -
Zoller Frederic,
Markert Annette,
Barthe Philippe,
Zhao Wenye,
Weichert Wilko,
Askoxylakis Vasileios,
Altmann Annette,
Mier Walter,
Haberkorn Uwe
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201203857
Subject(s) - phage display , peptide , peptide library , chemistry , in vivo , trypsin , biochemistry , scaffold , microbiology and biotechnology , computational biology , biology , peptide sequence , enzyme , computer science , genetics , database , gene
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.