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Optimized Fmoc solid‐phase synthesis of Thymosin α1 by side‐chain anchoring onto a PEG resin
Author(s) -
GarcíaRamos Yésica,
Giraud Matthieu,
TullaPuche Judit,
Albericio Fernando
Publication year - 2009
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21317
Subject(s) - chemistry , peptide , side chain , solid phase synthesis , polyethylene glycol , peptide synthesis , combinatorial chemistry , amino acid , peg ratio , thymosin , sequence (biology) , acetylation , peptide sequence , polymer chemistry , organic chemistry , biochemistry , polymer , finance , economics , gene
Thymosin α1 is a 28‐amino acid acetylated peptide used for the treatment of hepatitis B and C. This peptide has a difficult sequence because of the presence of consecutive β‐branched amino acids and shows a tendency to form β‐sheet structures, partly as a result of the many protecting groups required to assemble the peptide (up to 20 side‐chain protecting groups). Consequently, its synthesis has been generally achieved by convergent solution chemistry. Here we report a straightforward stepwise solid‐phase synthesis on a polyethylene glycol solid‐support that enables the scaling‐up of this key therapeutic peptide. © 2009 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 92: 565–572, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com