An insoluble graft copolymer consisting of the covalently bound polyoxyethylene to cross-linked polystyrene (HO-POE-PS) was prepared by anionic polymerization of ethylene oxide on the resin. The copolymer was then converted to the corresponding amino-polymer (H 2 N-POE-PS) and the latter was employed as the solid carrier for peptide synthesis. Although HO-POE-PS has successfully been employed as a carrier for peptide synthesis by the standard shaking procedure using /-butoxycarbonyl-amino acids, now we deemed it of interest to test its suitability for the continuous flow synthesis. Thus, the C-terminal octapeptide of the porcine insulin B chain (B23-30) was prepared by this procedure using a photolabile anchoring group and fluoren-9-ylmethoxycarbonyl-amino acids. All the reactions were carried out in a continuous flow manner in a steel column under pressure using a high-performance liquid chromatography (HPLC) system. At the end of the synthesis, a sample of the proiected peptide was cleaved from the support by photolysis. For the cleavage of another sample, an aqueous solution of sodium carbonate w*s employed. The protected peptide was purified on silica gel and Sephadex-LH 20. All the protecting groups of a sample of the octapeptide were removed with piperidine/dimethylformamide and trifluoroacetic acid and the deblocked peptide was purified by ion-exchange chiomatography. The free peptide was shown to be homogeneous by thin-layer chromatography, HPLC, and electrophoresis. The identify af the free octapeptide was confirmed by aminc-acid analysis, 13 C-nuclear magnetic resonance measurement and field-desorption mass spectiometry. The peptide was also shown to be free of racemization. Kontinuierliche Peptidsynthese auf dem Aminopolyoxyethylen-Polystyrol-Träger in einem Durchflußreaktor unter Verwendung der Fmoc-Strategie
Polystyrene-polyoxyethylene craft copolymers have been used for step-wise peptide synthesis. After completion of synthesis the protecting groups are cleaved under acidic conditions, where the polymer-peptide bond is stable. These gels in comparison to polystyrene peptide gels, show better properties for applications in affinity chromatography as well as synthesis on solid supports, because the advantageous properties of polystyrene beads are combined with the excellent spacer behavior of polyoxyethylene chains (mobility, solvation by water and organic solvents). Peptide gels with polylysine sequences have been synthesized as highly selective stationary phases for the separation of the homologous oligo desoxyribonucleotides (dT)n with n = 1-3. The principal possibilities of these gels for affinity chromatography is demonstrated.
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