Skip to main content

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

Buy Article:

$55.00 plus tax (Refund Policy)

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.
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

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

Document Type: Review Article

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

Publication date: 2003-12-01

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.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more