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Solid-Phase Synthesis of Structurally Diverse Scaffolded Peptides for the Mimicry of Discontinuous Protein Binding Sites

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Abstract:

Scaffolded peptides, in which fragments of the sequence are presented through a molecular scaffold in a discontinuous and nonlinear fashion, are promising candidates for the mimicry of discontinuous protein binding sites. Twelve scaffold molecules based on cyclic peptides with ring sizes ranging from 13 to 30 were generated. Up to three different peptide fragments were attached to the scaffolds in a site-selective manner, yielding scaffolded peptides in excellent purities, as documented by MS, HPLC, and 2D 1H NMR spectroscopy data.

Keywords: binding sites; discontinuous protein; molecular scaffold; scaffolded peptides; solid-phase synthesis

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866033478519

Affiliations: GBF - German Research Centre for Biotechnology, Mascheroder Weg 1, 38124 Braunschweig, Germany.

Publication date: December 1, 2003

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2003/00000010/00000006/art00001
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