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

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

Volume: 10 Issue: 6

Author(s): Raimo Franke, Christian Doll, Victor Wray and Jutta Eichler

Affiliation:

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

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.

Cite this article as:

Franke Raimo, Doll Christian, Wray Victor and Eichler Jutta, Solid-Phase Synthesis of Structurally Diverse Scaffolded Peptides for the Mimicry of Discontinuous Protein Binding Sites, Protein & Peptide Letters 2003; 10 (6) . https://dx.doi.org/10.2174/0929866033478519