The 2,4-dinitrophenyl group for protection of hydroxyl function of tyrosine during solid-phase peptide synthesis.
The facile thiolytic cleavage of the O-2,4-dinitrophenyl (Dnp) tyrosine bound was applied to the solid-phase synthesis of the 22-amino acid residue peptide H-Asp-Ala-Val-Tyr-Thr-Gly-Leu-Asn-Thr-Arg-Asn-Gln-Glu-Thr-Tyr-Glu-Thr-Le u-Lys- His-Glu-Lys-OH, corresponding to positions 62-83 in the chain of the type 1 receptor for Fc epsilon domains expressed on the rat mucosal-type mast cells (line RBL-2H3). A method for the spectrophotometric determination of insoluble O-Dnp as well as of unprotected phenolic moieties of tyrosine was developed. It is based on monitoring S-Dnp-2-mercaptoethanol, produced upon O-Dnp thiolysis by 2-mercaptoethanol.
Philosof-Oppenheimer
R
R
Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Pecht
I
I
Fridkin
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D004136:Dinitrobenzenes / Q000737:chemistry; D008623:Mercaptoethanol / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D051381:Rats; D017455:Receptors, IgE / Q000737:chemistry; D013053:Spectrophotometry; D014443:Tyrosine / Q000737:chemistry*
D004136:Dinitrobenzenes; D010455:Peptides; D017455:Receptors, IgE; D014443:Tyrosine; D008623:Mercaptoethanol