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 language | English (US) |
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Pages (from-to) | 168-180 |
Number of pages | 13 |
Journal | Journal of Peptide Science |
Volume | 3 |
Issue number | 3 |
DOIs | |
State | Published - 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