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Molecules 2011, 16(3), 2467-2485; doi:10.3390/molecules16032467

Miniproteins as Phage Display-Scaffolds for Clinical Applications

1 Clinical Cooperation Unit Nuclear Medicine, German Cancer Research Center, INF 280, 69120 Heidelberg, Germany 2 Department of Nuclear Medicine, University Hospital Heidelberg, INF 400, 69120 Heidelberg, Germany
* Author to whom correspondence should be addressed.
Received: 23 December 2010 / Revised: 4 March 2011 / Accepted: 7 March 2011 / Published: 14 March 2011
(This article belongs to the Special Issue Phage Display of Combinatorial Libraries)
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Miniproteins are currently developed as alternative, non-immunoglobin proteins for the generation of novel binding motifs. Miniproteins are rigid scaffolds that are stabilised by alpha-helices, beta-sheets and disulfide-constrained secondary structural elements. They are tolerant to multiple amino acid substitutions, which allow for the integration of a randomised affinity function into the stably folded framework. These properties classify miniprotein scaffolds as promising tools for lead structure generation using phage display technologies. Owing to their high enzymatic resistance and structural stability, miniproteins are ideal templates to display binding epitopes for medical applications in vivo. This review summarises the characteristics and the engineering of miniproteins as a novel class of scaffolds to generate of alternative binding agents using phage display screening. Moreover, recent developments for therapeutic and especially diagnostic applications of miniproteins are reviewed.
Keywords: phage display; miniprotein; scaffold; in vivo diagnostics; protein engineering phage display; miniprotein; scaffold; in vivo diagnostics; protein engineering
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Zoller, F.; Haberkorn, U.; Mier, W. Miniproteins as Phage Display-Scaffolds for Clinical Applications. Molecules 2011, 16, 2467-2485.

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