Binding sugars: from natural lectins to synthetic receptors and engineered neolectins

Chem Soc Rev. 2013 Jun 7;42(11):4798-813. doi: 10.1039/c2cs35435g. Epub 2013 Jan 25.

Abstract

The large diversity and complexity of glycan structures together with their crucial role in many biological or pathological processes require the development of new high-throughput techniques for analyses. Lectins are classically used for characterising, imaging or targeting glycoconjugates and, when printed on microarrays, they are very useful tools for profiling glycomes. Development of recombinant lectins gives access to reliable and reproducible material, while engineering of new binding sites on existing scaffolds allows tuning of specificity. From the accumulated knowledge on protein-carbohydrate interactions, it is now possible to use nucleotide and peptide (bio)synthesis for producing new carbohydrate-binding molecules. Such a biomimetic approach can also be addressed by boron chemistry and supra-molecular chemistry for the design of fully artificial glycosensors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aptamers, Nucleotide / chemistry
  • Aptamers, Nucleotide / metabolism
  • Aptamers, Peptide / chemistry
  • Aptamers, Peptide / metabolism
  • Boronic Acids / chemistry
  • Glycoconjugates / chemistry
  • Glycoside Hydrolases / metabolism
  • Lectins / chemistry
  • Lectins / metabolism*
  • Oligonucleotides / chemistry
  • Oligonucleotides / metabolism
  • Peptides / chemistry
  • Peptides / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Engineering

Substances

  • Aptamers, Nucleotide
  • Aptamers, Peptide
  • Boronic Acids
  • Glycoconjugates
  • Lectins
  • Oligonucleotides
  • Peptides
  • Polysaccharides
  • Glycoside Hydrolases