Construction and application of a new class of sequential oligopeptide carriers (SOCn) for multiple anchoring of antigenic peptides-application to the acetylcholine receptor (AChR) main immunogenic region
| Autor: | Socrates J. Tzartos, Efstratia H. Vatzaki, Michel Marraud, Maria Sakarellos-Daitsiotis, Vassilios Tsikaris, Piotr Orlewski, Constantinos Sakarellos, Manh Thong Cung |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Oligopeptide Magnetic Resonance Spectroscopy Protein Conformation Stereochemistry Chemistry Antibodies Monoclonal Anchoring General Medicine Biochemistry Peptide Conformation Epitopes Molecular dynamics Nicotinic acetylcholine receptor Molecular recognition Structural Biology otorhinolaryngologic diseases Humans Receptors Cholinergic Structural motif Oligopeptides Molecular Biology Acetylcholine receptor |
| Zdroj: | International Journal of Biological Macromolecules. 19:195-205 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/0141-8130(96)01128-2 |
| Popis: | A new class of sequential oligopeptide carriers (SOC n ), namely (Lys-Aib-Gly) n ( n = 2–7), for anchoring antigenic peptides, is presented. These SOC n have been designed in order to assume a determined structural motif, exhibiting defined spatial orientations of the Lys-N e H 2 anchoring groups. The NMR study showed that SOC n 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 1 HNMR, that all the antigenic peptides bound to the SOC n , 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 SOC n , impose a favorable disposition of the anchored peptides so that potent antigens with maximum molecular recognition are generated. |
| Databáze: | OpenAIRE |
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