Solid‐phase synthesis of peptides with C‐terminal asparagine or glutamine: An effective, mild procedure based on Nx‐fluorenylmethyloxycarbonyl (Fmoc) protection and side‐chain anchoring to a tris(alkoxy)benzylamide (PAL) handle

FERNANDO ALBERICIO, ROBERT VAN ABEL, GEORGE BARANY

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29 Scopus citations

Abstract

Attempts to anchor Fmoc‐asparagine or glutamine as p‐alkoxybenzyl esters for solid‐phase peptide synthesis are fraught with difficulties. A convenient and effective method to prepare peptides with C‐terminal asparagine or glutamine involves quantitative attachment of Nx ‐Fmoc‐Cx ‐tert.‐butyl aspartate or glutamate via the free ω‐carboxyl groups to a tris(alkoxy)benzylamino (PAL) support. Chain elongation proceeds normally by standard Fmoc chemistry, and treatment with acid, e.g., CF3COOH—CH2Cl2, 90 min at 25°, releases the desired peptides in >95% yields without side reactions at the C‐terminus. Feasibility of the approach has been demonstrated by the syntheses of the C‐terminal octapeptide from human proinsulin, H‐Leu‐Ala‐Leu‐Glu‐Gly‐Ser‐Leu‐Gin‐OH, and the serum thymic factor pGlu‐Ala‐Lys‐Ser‐Gln‐Gly‐Gly‐Ser‐Asn‐OH.

Original languageEnglish (US)
Pages (from-to)284-286
Number of pages3
JournalInternational Journal of Peptide and Protein Research
Volume35
Issue number3
DOIs
StatePublished - Mar 1990

Keywords

  • C‐terminal asparagine
  • C‐terminal glutamine
  • N‐fluorenylmethyloxycarbonyl (Fmoc) amino acids
  • side‐chain anchoring
  • solid‐phase peptide synthesis
  • tris(alkoxy)benzylamide (PAL) handle

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