Ser-His catalyses the formation of peptides and PNAs

Maçha Gorlero, Rafal Wieczorek, Katarzyna Adamala, Alessandra Giorgi, Maria Eugenia Schininà, Pasquale Stano, Pier Luigi Luisi

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

The dipeptide seryl-histidine (Ser-His) catalyses the condensation of esters of amino acids, peptide fragments, and peptide nucleic acid (PNA) building blocks, bringing to the formation of peptide bonds. Di-, tri- or tetra-peptides can be formed with yields that vary from 0.5% to 60% depending on the nature of the substrate and on the conditions. Other simpler peptides as Gly-Gly, or Gly-Gly-Gly are also effective, although less efficiently. We discuss the results from the viewpoint of primitive chemistry and the origin of long macromolecules by stepwise fragment condensations.

Original languageEnglish (US)
Pages (from-to)153-156
Number of pages4
JournalFEBS Letters
Volume583
Issue number1
DOIs
StatePublished - Jan 5 2009
Externally publishedYes

Bibliographical note

Funding Information:
Research conducted in the P.L.L.’s laboratory (Chemical Synthetic Biology) is supported by the EC FP6 (contract #043359), the Human Frontier Science Program, and the Italian Space Agency.

Keywords

  • Fragment condensation
  • Organocatalysis
  • Origins of life
  • Peptide condensation
  • Prebiotic chemistry

Fingerprint Dive into the research topics of 'Ser-His catalyses the formation of peptides and PNAs'. Together they form a unique fingerprint.

Cite this