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Sunflower trypsin inhibitor 1 derivatives as molecular scaffolds for the development of novel peptidic radiopharmaceuticals

Peptides with restricted conformation provide increased affinity and stability against degradation as compared to linear peptides. This study investigates the characteristics of derivatives of the sunflower trypsin inhibitor 1 (SFTI-1), a 14 amino acid peptide with high intrinsic stability.

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Bibliographic Details
Main Authors: Garcia Boy, Regine (Author) , Mier, Walter (Author) , Nothelfer, Eva-Maria (Author) , Altmann, Annette (Author) , Eisenhut, Michael (Author) , Kolmar, Harald (Author) , Tomaszowski, Michael (Author) , Krämer, Susanne (Author) , Haberkorn, Uwe (Author)
Format: Article (Journal)
Language:English
Published: 2010
In: Molecular imaging & biology
Year: 2010, Volume: 12, Issue: 4, Pages: 377-385
ISSN:1860-2002
DOI:10.1007/s11307-009-0287-z
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s11307-009-0287-z
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Author Notes:Regine García Boy, Walter Mier, Eva Maria Nothelfer, Annette Altmann, Michael Eisenhut, Harald Kolmar, Michael Tomaszowski, Susanne Krämer, Uwe Haberkorn
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Summary:Peptides with restricted conformation provide increased affinity and stability against degradation as compared to linear peptides. This study investigates the characteristics of derivatives of the sunflower trypsin inhibitor 1 (SFTI-1), a 14 amino acid peptide with high intrinsic stability.
Item Description:Erstmals am 24. November 2009 online veröffentlicht
Gesehen am 15.02.2023
Physical Description:Online Resource
ISSN:1860-2002
DOI:10.1007/s11307-009-0287-z

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