Insertion of foreign epitopes in HBcAg: how to make the chimeric particle assemble

Citation
Li. Karpenko et al., Insertion of foreign epitopes in HBcAg: how to make the chimeric particle assemble, AMINO ACIDS, 18(4), 2000, pp. 329-337
Citations number
26
Categorie Soggetti
Biochemistry & Biophysics
Journal title
AMINO ACIDS
ISSN journal
09394451 → ACNP
Volume
18
Issue
4
Year of publication
2000
Pages
329 - 337
Database
ISI
SICI code
0939-4451(2000)18:4<329:IOFEIH>2.0.ZU;2-L
Abstract
Hepatitis B core antigen is one of the most promising protein carriers of f oreign epitopes of various human and animal pathogens. Chimeric HBcAg parti cles can be used as effective artificial immunogenes. Unfortunately, not al l chimeric proteins are able to be particulated. The dependence of correct or incorrect folding of chimeric proteins on physical and chemical properti es of inserts was studied with the help of ProAnalyst, SALIX and QSARPro co mputer programs. We have found that insertion of amino acids with high hydr ophobicity, large volume, and high beta-strand index prevent self-assemblin g chimeric proteins. These factors are most important for the C-termini of inserts. Recommendations for obtaining correct folding of chimeric HBcAg pa rticles have been given.