Abstrakt

Solid-phase synthesis of partial sequences of rubber elongation factor protein on hexanediol diacrylate crosslinked polystyrene support

V.N.Subha, M.P.Sooraj, M.Beena

Peptide synthesis has presently emerged as a powerful tool for studying protein/peptide structures and their functions, initiating biomedical researches in immunology, pharmacology, enzymology and molecular biology. Peptides are present in very small amount in their biological sources and it is very difficult to isolate and purify them. The invention of SPPS is the real land mark in synthetic peptide chemistry. Though many modifications have been done on Merrifield synthesis, many a peptide chains, particularly hydrophobic peptide chains have not been prepared successfully using this method. The difficulties observed in the synthesis can be attributed to change in solvation of the peptide-polymer at different stages in the synthesis giving rise to both truncated and deletion sequences.Also, the strong association of hydrophobic peptides via â-sheet formation within the peptide-polymer matrix is a major problem. Herein we report the synthesis and usage of 2% hexanediol diacrylate-crosslinked polystyrene support for the production of highly hydrophobic peptides. The synthetic utility of the support was demonstrated by the quantitative synthesis of the hydrophobic fragments of rubber elongation factor protein on the chloromethylated support. The first successful attempt to synthesize partial sequences of REF protein by solid phase peptide synthesis is reported. The free peptide was obtained in high yield and purity as checked by reverse phase HPLC. The synthesized peptides were characterized by amino acid analysis and electronspray ionization mass spectrometry.