Premium
The structural and aggregation properties of the synthetic C‐terminal half (104‐mer) polypeptide from HIV p24gag resemble those of full‐length protein
Author(s) -
Ball Haydn L.,
Chan A. W. Edith,
Gibbons William A.,
Coates Anthony R. M,
Mascagni Paolo
Publication year - 1997
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199705)3:3<168::aid-psc95>3.0.co;2-p
Subject(s) - tetramer , dimer , monomer , chemistry , peptide , sequence (biology) , stereochemistry , aqueous solution , protein aggregation , biochemistry , polymer , organic chemistry , enzyme
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 p I 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. © 1997 European Peptide Society and John Wiley & Sons, Ltd.