The structural and aggregation properties of the synthetic C-terminal half (104-mer) polypeptide from HIV p24gag resemble those of full-length protein

Haydn L. Ball, A. W Edith Chan, William A. Gibbons, Anthony R M Coates, Paolo Mascagni

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

The aggregation and structural properties of the synthetic C-terminal half [Ala330, Ala350)270-373; 104-mer)] polypeptide from HIV-1 p24gag were studied. In concentrated solutions the synthetic polypeptide aggregated to tetramers which, upon dilution, gave a mixture of monomeric and dimeric species. These results correlated well with the in vitro aggregation properties of recombinant p24. The tetrameric form of the synthetic polypeptide had a pI which differed by about four units from that of the mixture of monomeric and dimeric species. CD studies indicated that the latter contained, in aqueous solutions, a compact molecule lacking, however, a defined tertiary structure. Addition of MeOH to aqueous solutions of both tetramer and monomer/ dimer mixture induced a more defined structure, which was assigned to that of an α + β protein in agreement with secondary structure predictions. A model of the dimeric form of the 104-mer, which takes into account the results presented here and those from a study on the specificity of a set of anti-104-mer MoAbs, is presented. Finally, the results indicated that the structure of the 104-mer in its dimeric form is similar to that adopted by the same sequence when part of full-length p24.

Original languageEnglish (US)
Pages (from-to)168-180
Number of pages13
JournalJournal of Peptide Science
Volume3
Issue number3
StatePublished - May 1 1997

Keywords

  • CD spectroscopy
  • HIV
  • Secondary-structure prediction
  • Synthetic proteins
  • p24

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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