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.