Premium
High‐yield, solid‐phase synthesis of humanin, an Alzheimer's disease associated, novel 24‐mer peptide which contains a difficult sequence
Author(s) -
Evangelou Alexandra,
Zikos Christos,
Livaniou Evangelia,
Evangelatos Gregory P.
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.572
Subject(s) - peptide , sequence (biology) , neurotoxicity , combinatorial chemistry , potency , yield (engineering) , peptide synthesis , computational biology , chemistry , residue (chemistry) , biochemistry , biology , in vitro , materials science , toxicity , organic chemistry , metallurgy
Humanin is a novel, 24‐mer residue bioactive peptide, which antagonizes Alzheimer's disease (AD) related neurotoxicity and offers a hope for developing new therapeutics against AD. Access to adequate amounts of pure humanin is a prerequisite for further, thorough, investigation of the pharmacological properties and therapeutic potency of the peptide. Until now, humanin has been obtained mainly by molecular biology techniques. In this work the Fmoc solid‐phase synthesis of humanin on an in‐house prepared 2‐Cl‐tritylamidomethyl polystyrene resin is described fully. Special precautions, i.e. prolonged deprotection steps, should be taken to achieve a high overall yield, since humanin seems to contain a ‘difficult sequence’ (R 4 G 5 F 6 S 7 C 8 L 9 ) near its highly lipophilic, biologically important region L 9 L 10 L 11 L 12 . Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.