Open AccessThis article is
- freely available
Miniproteins as Phage Display-Scaffolds for Clinical Applications
Clinical Cooperation Unit Nuclear Medicine, German Cancer Research Center, INF 280, 69120 Heidelberg, Germany
Department of Nuclear Medicine, University Hospital Heidelberg, INF 400, 69120 Heidelberg, Germany
* Author to whom correspondence should be addressed.
Received: 23 December 2010; in revised form: 4 March 2011 / Accepted: 7 March 2011 / Published: 14 March 2011
Abstract: 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
Citations to this Article
Cite This Article
MDPI and ACS Style
Zoller, F.; Haberkorn, U.; Mier, W. Miniproteins as Phage Display-Scaffolds for Clinical Applications. Molecules 2011, 16, 2467-2485.
Zoller F, Haberkorn U, Mier W. Miniproteins as Phage Display-Scaffolds for Clinical Applications. Molecules. 2011; 16(3):2467-2485.
Zoller, Frederic; Haberkorn, Uwe; Mier, Walter. 2011. "Miniproteins as Phage Display-Scaffolds for Clinical Applications." Molecules 16, no. 3: 2467-2485.