Skok M V, Lykhmus O Yu, Bobrovnik S O, Solodova O V, Tzartos S J, Tsouloufis T, Vanderesse R, Marraud M
Palladin Institute of Biochemistry, NAS of Ukraine, Kyiv.
Ukr Biokhim Zh (1999). 2002 Jul-Aug;74(4):54-60.
The antibodies to nicotinic acetylcholine receptor alpha(181-192) synthetic peptides were elicited in rabbits and mice using the peptides conjugated to protein carriers in different orientations, either through C-terminal Cys (S-conjugates), or through amino groups (N-conjugates). S-conjugated peptides were less potent in eliciting peptide-specific antibodies compared to N-conjugates and this type of conjugation resulted in antibodies to the coupling reagent. However, the epitopes present in either S- or N-conjugated peptides appeared to be similar, indicating that amino acid residues, which form the epitope, were located in the middle part of the peptide and did not include both N- and C-terminal residues. Peptide conjugation to a protein carrier did not play a role in stabilizing the peptide conformation, but was necessary to concentrate the peptide epitopes on the carrier surface enabling bivalent antibody binding.
使用以不同方向与蛋白质载体偶联的肽，即通过C末端半胱氨酸（S-偶联物）或通过氨基（N-偶联物），在兔和小鼠中引发针对烟碱型乙酰胆碱受体α(181 - 192)合成肽的抗体。与N-偶联物相比，S-偶联肽引发肽特异性抗体的能力较弱，并且这种偶联类型会产生针对偶联试剂的抗体。然而，S-或N-偶联肽中存在的表位似乎相似，这表明形成表位的氨基酸残基位于肽的中间部分，不包括N-和C-末端残基。肽与蛋白质载体的偶联在稳定肽构象方面不起作用，但对于将肽表位集中在载体表面以实现二价抗体结合是必要的。
