A new helicoid-type sequential oligopeptide carrier (SOC(n)) for developing potent antigens and immunogens.
A new class of sequential oligopeptide carriers (SOC(n)) for anchoring antigenic/immunogenic peptides has been constructed. The carrier, formed by the repetitive Lys-Aib-Gly moiety, is designed to display a predetermined 3D structure, so that the attached peptides would obtain a defined spatial orientation. Conformational analysis showed that SOC(n) adopt a distorted 3(10)-helical structure, while the coupled peptides preserve their original 'active' structure. Coupling to the carrier may also result to the enhancement of one conformer of the anchored peptide. It is concluded that the structure of SOC(n) offers an optimal presentation of the attached peptides, so that potent antigens or immunogens are generated.
Sakarellos-Daitsiotis
M
M
Department of Chemistry, Section of Organic Chemistry and Biochemistry, University of Ioannina, 45110, Ioannina, Greece.
Tsikaris
V
V
Sakarellos
C
C
Vlachoyiannopoulos
P G
PG
Tzioufas
A G
AG
Moutsopoulos
H M
HM
D000595:Amino Acid Sequence; D000941:Antigens / Q000276:immunology*; D004337:Drug Carriers; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014614:Vaccines, Synthetic / Q000276:immunology*
D000941:Antigens; D004337:Drug Carriers; D009842:Oligopeptides; D014614:Vaccines, Synthetic