Sodium dodecyl 2-hydroxy-3-chloropropy1 phosphate (C
12-AHCP-Na) was synthesized by the reaction of sodium dodecyl hydrogenphosphate (C
12-MAP) and 1, 2-epo. xy-3-chloropropane. (Fig.1, Scheme 1, A), Sodium dodecyl 2, 3-epoxypropyl phosphate (C
12-AGP-Na) was obtained quantitatively by the treatment of C
12-AHCP-Na with equivalent amount of NaOH. '(Scheme 1, B) C
12-AGP-Na is an amphiphilic Phosphoric acid ester containing a reactive ep oxyring, which can react with various active hydrogen compounds. The reactions of C
12-AGP-Na with some am ino acids (glycine, N-methylglycine and Lcysteine)were studied, and new amphiphilic amino acid derivatives of MAP 1, 2 and 3 were obtained. (Scheme 2) In, the Teact, ion of C
12-A. GP-Na with glycipe in aqueous solution, the hydrolysis of C
12-AGP-Na, which gave sodium dodecyl- glyceryl phosphate (C
12-AGCP-Na), was unavoidable, but with the equirnolar amount of L-cysteine in aqueous solu tion, L-cysteine derivatives of MAP were obtained quantitatively.
By the analysis of the NMR spectra of 3 it was suggested that th e, ring opening of the epoxide of C
12-AGP-Na was the selective β-fission by the -SH group of L-cysteine. From the studies on the reactivity of C
12-AGP with HS-CH
2CH
2-OH, H
2N-CH
2-CH
2-OH, and OH-CH
2C11
2-OH in the dilute borate buffer solution (pH=9.5), the order of reactivity of tthe. active hydrogen groups for the epoxide of C
12-AGP-Na was -SH>-NH
2>-OH (-OH had no reactivity). The m odification of BSA (Bovine Serum Albumin) with C
12-AGP-Na in the dilute borate buffer solution (pH=9.5) was studied. From the SDS-polyacrylarnide gel electrophoresis analysis (Fig.2),
31P-NMR spectrum analysis, and the free -NH
2 group determination, it was found that BSA was effectively modified with C
12-AGP-Na and this suggests that AGP can be applicable to protein and peptide for as a new type of modifier. The Reaction of Epoxy-compoundw itht Phosphate. III.
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