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Heterobifunctionalized tetraethylene glycol: A spacer for surface attachment of viral peptide epitopes for ELISA and derivatization of membrane modifying peptides

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Abstract

New hydrophilic linkers of the formula Fmoc- NHCH2CH2COO(CH2CH2O)4X (X = COCH2CH2COOH Fmoc-Ats (2), X = CONHCH2COOH Fmoc-Atg (4), and X = CONHCH2CH2COOH Fmoc-Ata (5)) have been prepared by heterobifunctional modification of tetraethylene glycol as starting material. These linkers represent a useful tool for solid phase peptide synthesis according to Fmoc/tBu strategy. Two examples are presented to illustrate the applicability of these building blocks: (i) spacing between biotin and a peptide epitope of the hepatitis C virus and evaluation in a biotin- streptavidin ELISA, and (ii) coupling of the new linker to the N- and C-terminus of the peptide antibiotic alamethicin to show eventual influences on the peptide's α-helical conformation.

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Correspondence to Günther Jung.

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Mack, J., Kienle, S., Leipert, D. et al. Heterobifunctionalized tetraethylene glycol: A spacer for surface attachment of viral peptide epitopes for ELISA and derivatization of membrane modifying peptides. Letters in Peptide Science 6, 135–142 (1999). https://doi.org/10.1023/A:1008890613419

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  • DOI: https://doi.org/10.1023/A:1008890613419

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