Syntheses of four peptides from the immunodominant region of hepatitis C viral pathogens using PS-TTEGDA support for the investigation of HCV infection in human blood

Citation
Ks. Kumar et al., Syntheses of four peptides from the immunodominant region of hepatitis C viral pathogens using PS-TTEGDA support for the investigation of HCV infection in human blood, J PEPT RES, 56(2), 2000, pp. 88-96
Citations number
19
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF PEPTIDE RESEARCH
ISSN journal
1397002X → ACNP
Volume
56
Issue
2
Year of publication
2000
Pages
88 - 96
Database
ISI
SICI code
1397-002X(200008)56:2<88:SOFPFT>2.0.ZU;2-#
Abstract
Four peptides were designed and synthesized on a highly solvating copolymer of tetraethyleneglycol diacrylate cross-linked polystyrene (PS-TTEGDA) sup port with very high purity and yield. The polymer was synthesized in variou s crosslinking densities (1, 2, 3, 4 5 and 10%) using radical aqueous suspe nsion polymerization. Four per cent PS-TTEGDA resin showed rigidity and mec hanical characteristics comparable with those of divinylbenzene cross-linke d polystyrene (PS-DVB) support. Swelling and solvation characteristics of P S-TTEGDA were much higher than PS-DVB support in all solvents used in solid -phase peptide synthesis. Forty-eight hour treatment of the support with ne at trifluoroacetic acid did not show any change in its infrared spectra. PS -TTEGDA could be functionalized with chloromethyl, aminomethyl and hydroxym ethyl functional groups under various controlled conditions. Synthetic util ity of the support was demonstrated by the synthesis of four peptides selec ted from the envelope and nonstructural protein region of the prototype hep atitis C virus (HCV). These peptides were later used successfully to develo p a peptide-based immunoassay (PBEIA) for the detection of HCV immunity. Pe ptides designed from the NS1 and N54 protein regions were found to be very promising for the development of a new diagnostic kit to detect HCV infecti on in human blood. Peptide purity was tested by RP-FPLC and the peptide ide ntity was confirmed by amino acid analysis.