Jt. Varkey et Vnr. Pillai, SYNTHESIS OF THIOREDOXIN PARTIAL SEQUENCES ON 1,6-HEXANEDIOL DIACRYLATE (HDODA)-CROSS-LINKED POLYSTYRENE RESIN, The journal of peptide research, 51(1), 1998, pp. 49-54
The continued and rapid discoveries of new peptides with interesting b
iological functions have created an unprecedented demand for the chemi
cal synthesis of peptides required for structure-function correlations
. Several strategic improvements have been suggested and tested to mee
t the demand for peptides in high purity and quantity. This article de
scribes the synthesis of three partial sequences of thioredoxin, a nat
urally occurring sulfur-reducing protein containing 108 amino acid res
idues, on a newly developed flexible, cross-linked polystyrene support
(2% polystyrene cross-linked with 1,6-hexanediol diacrylate) using th
e standard solid-phase methodology. The protected peptides were cleave
d from the polymeric support by trifluoroacetic acid and purified by c
hromatography. The free peptides were shown to be homogeneous by high-
performance liquid chromatography and were characterized by amino acid
analysis and circular dichroism. The circular dichroism measurement r
evealed that the peptides possess a helical conformation. From the yie
ld and purity of the peptides obtained, it was inferred that the favor
able swelling and solvation characteristics of the support facilitated
effective synthesis. (C) Munksgaard 1997.