A new protecting group for tryptophan in solid-phase peptide synthesis which protectsagainst acid-catalyzed side reactions and facilitates purification by HPLC
2009 (English)In: Tetrahedron Letters, ISSN 0040-4039, E-ISSN 1359-8562, Vol. 50, no 24, 2976-2978 p.Article in journal (Refereed) Published
The indole nucleus of Z-Trp-OBzl is modified by acylation of the indole nitrogen using Boc-N-methyl butyric acid followed by catalytic hydrogenation and introduction of the Fmoc group. The resulting derivative, Fmoc-Trp(Boc-Nmbu)-OH, is incorporated into peptide chains via solid-phase peptide synthesis (SPPS). After assembly of the peptide chain, the Boc group is cleaved by treatment with TFA. The peptide is isolated with the tryptophan residue modified with a cationic 4-(N-methylamino) butanoyl group, which improves the solubility of the peptide during HPLC purification. On treatment of the purified peptide at pH 9.5, the Nmbu group undergoes an intramolecular cyclization reaction; this results in the fully deprotected peptide and N-methylpyrrolidone.
Place, publisher, year, edition, pages
2009. Vol. 50, no 24, 2976-2978 p.
IdentifiersURN: urn:nbn:se:su:diva-27554DOI: 10.1016/j.tetlet.2009.04.014ISI: 000266188300036OAI: oai:DiVA.org:su-27554DiVA: diva2:214747