The structural and aggregation properties of the synthetic C-terminal half (104-mer) polypeptide from HIV p24gag resemble those of full-length protein
✍ Scribed by Haydn L. Ball; A. W. Edith Chan; William A. Gibbons; Anthony R. M Coates; Paolo Mascagni
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 261 KB
- Volume
- 3
- Category
- Article
- ISSN
- 1075-2617
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✦ Synopsis
The aggregation and structural properties of the synthetic C-terminal half [Ala 330 , Ala 350 )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 a b 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.