Tsikaris V, Sakarellos C, Sakarellos-Daitsiotis M, Orlewski P, Marraud M, Cung M T, Vatzaki E, Tzartos S
Department of Chemistry, University of Ioannina, Greece.
Int J Biol Macromol. 1996 Oct;19(3):195-205. doi: 10.1016/0141-8130(96)01128-2.
A new class of sequential oligopeptide carriers (SOCn), namely (Lys-Aib-Gly)n (n = 2-7), for anchoring antigenic peptides, is presented. These SOCn have been designed in order to assume a determined structural motif, exhibiting defined spatial orientations of the Lys-N epsilon H2 anchoring groups. The NMR study showed that SOCn adopt a rigid conformation with some regularity, initiated from the C-terminus of the carrier, while molecular dynamics simulation confirmed the occurrence of a distorted 3(10)-helix. It was also demonstrated, by 1HNMR, that all the antigenic peptides bound to the SOCn retain their original, folded active, structure and that probably they do not interact to each other. It is concluded that the beneficial structural elements of the SOCn impose a favorable disposition of the anchored peptides so that potent antigens with maximum molecular recognition are generated.
本文介绍了一类用于锚定抗原肽的新型序列寡肽载体(SOCn),即(Lys-Aib-Gly)n(n = 2 - 7)。设计这些SOCn是为了呈现特定的结构基序,使Lys-NεH2锚定基团具有明确的空间取向。核磁共振(NMR)研究表明,SOCn从载体的C端开始有一定规律地呈现刚性构象,而分子动力学模拟证实了扭曲的3(10)-螺旋的存在。通过1H NMR还证明,所有与SOCn结合的抗原肽都保留了其原始的折叠活性结构,并且它们之间可能不相互作用。结论是,SOCn的有益结构元件使锚定肽具有良好的排列方式,从而产生具有最大分子识别能力的强效抗原。