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Synthesis and fluorescent labeling of beta‐amyloid peptides
Author(s) -
Fülöp Lívia,
Penke Botond,
Zarándi Márta
Publication year - 2001
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.346
Subject(s) - chemistry , fluorophore , peptide , fluorescence , fluorescein , amino acid , fluorescein isothiocyanate , isothiocyanate , peptide sequence , biochemistry , combinatorial chemistry , physics , quantum mechanics , gene
Fluorescent cell analytical techniques require the incorporation of a fluorophore into the target molecule without causing a significant change in the native conformation. Many short peptides have a limited number of reactive groups that can be labeled without affecting the biological activity. In this work we present several methods for labeling β‐amyloid peptides (βA[25–35], βA[1–40]) and their derivatives (LPFFD, RIIGL and RVVIA) with different chromophores exclusively at the N ‐terminus. In the case of liquid‐phase labeling, fluorescein isothiocyanate was used. The side‐chain amino function of Lys, if present in the sequence, was protected with an Fmoc group, whereby the hydrophobic character of the peptide was further increased. The labeling reaction was carried out in an appropriate deaggregating solvent, DMSO. For solid‐phase labeling, 5(6)‐carboxyfluorescein and 7‐amino‐4‐methyl‐3‐coumarinylacetic acid were applied. Several cleavage cocktails were tested for removal of the labeled amyloid peptides from the resin in order to completely suppress the oxidation of Met. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.