Chemical Synthesis of Ns-1 Region of Hepatitis C-Viral Polyprotein Fragments: A Comparison of Ps-Bdodma Resin and Merrifield Resin

Authors: Roice M.; Kumar K.Santhosh; Pillai V.N.Rajasekharan

Source: Protein and Peptide Letters, Volume 9, Number 3, June 2002 , pp. 245-252(8)

Publisher: Bentham Science Publishers

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Abstract:

Three peptide fragments selected from the NS-1 region of hepatitis C-viral polyprotein(Leu-Ile-Asn-Thr-Asn-Ala-Ser-Trp-His-Ala-Asn-Arg-Thr-Ala-Leu-Ser-Asn-Asp-Ser-Lys-Leu-Asn-Thr-Gly-Ala-NH2, Leu-lle-Asn-Thr-Asn-Ala-Ser-Trp-His-Ala-Asn-Arg-Thr-Ala-NH2 and Leu-Asn-Cys(Acm)-Asn-Asp-Ser-Leu-Asn-Thr-Ala-NH2) [1] have been synthesized on PS-BDODMA resin. The synthetic capability of the resin PS-BDODMA resin was compared with Merrifield resin. The peptides were synthesized by the stepwise fluoren-9-yl methoxycarbonyl (Fmoc) solid-phase method. The synthesized peptides were purified by HPLC and the identity of the peptides was established by mass spectrum and amino acid analysis. The synthesis of these peptides illustrates the application of the PS-BDODMA resin for the synthesis of long chain peptides in high yield and homogeneity compared to the Merrifield resin.

Keywords: hcv-polyprotein; solid phase synthesis; ps-bdodma; merrifield resin

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408788

Publication date: 2002-06-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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