Engineering Short Preorganized Peptide Sequences for Metal Ion Coordination: Copper(II) a Case Study

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Peptides are multidentate chiral ligands capable of coordinating different metal ions. Nowadays, they can be obtained with high yield and purity, thanks to the advances on peptide/protein chemistry as well as in equipment (peptide synthesizers). Based on the identity and length of their amino acid sequences, peptides can present different degrees of flexibility and folding. Although short peptide sequences (< 20 amino acids) usually lack structure in solution, different levels of structural preorganization can be induced by introducing conformational constraints, such as β-turn/loop template sequences and backbone cyclization. For all these reasons, and the fact that one is not restricted to use proteinogenic amino acids, small peptidic scaffolds constitute a simple and versatile platform for the development of inorganic systems with tailor-made properties and functions. Here we outline a general approach to the design of short preorganized peptide sequences (10–16 amino acids) for metal ion coordination. Based on our experience, we present a general scheme for the design, synthesis, and characterization of these peptidic scaffolds and provide protocols for the study of their metal ion coordination properties.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherElsevier Academic Press Inc
Pages333-364
Number of pages32
Volume580
DOIs
Publication statusPublished - 2016

Publication series

NameMethods in Enzymology
Volume580
ISSN (Print)00766879
ISSN (Electronic)15577988

Keywords

  • Coordination chemistry
  • Copper
  • Cyclic peptides
  • Metallopeptides
  • Preorganized structures
  • β-Turns

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