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 Citations (Scopus)

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 1997

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Agglomeration
HIV
Peptides
Proteins
Dimers
Dilution
HIV-1
Structural properties
Monomers
Molecules
In Vitro Techniques

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Analytical Chemistry

Cite this

The structural and aggregation properties of the synthetic C-terminal half (104-mer) polypeptide from HIV p24gag resemble those of full-length protein. / Ball, Haydn L.; Chan, A. W Edith; Gibbons, William A.; Coates, Anthony R M; Mascagni, Paolo.

In: Journal of Peptide Science, Vol. 3, No. 3, 05.1997, p. 168-180.

Research output: Contribution to journalArticle

Ball, Haydn L. ; Chan, A. W Edith ; Gibbons, William A. ; Coates, Anthony R M ; Mascagni, Paolo. / The structural and aggregation properties of the synthetic C-terminal half (104-mer) polypeptide from HIV p24gag resemble those of full-length protein. In: Journal of Peptide Science. 1997 ; Vol. 3, No. 3. pp. 168-180.
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