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• W1525192669 endingPage "164" @default.
• W1525192669 startingPage "159" @default.
• W1525192669 abstract "A cyclic disulfide peptide representing antigenic site A of foot-and-mouth-disease virus (FMDV) strain C-S8cl (residues 134 to 155 of viral protein l (VP1) with Tyr136 and Arg153 replaced by cystine; TTCTASARGDLAHLTTTHACHL) was synthesized by solid phase methods. Formation of the cyclic disulfide was carried out by air oxidation of the fully deprotected and reduced bis-cysteine precursor, under high dilution conditions. The identity of the cyclic peptide was confirmed by both physical and enzymatic methods. A conformational study of the cyclic peptide and of its linear parent structure (YTASARGDLAHLTTTHARHLP, residues 136–156 of VP1 of FMDV C-S8cl) by circular dichroism in the presence of a structure-inducing solvent showed the cyclic disulfide analog to adopt lower levels of α-helix than its linear counterpart. In competitive ELISA assays both peptides reacted with similar affinity against a representative panel of neutralizing monoclonal antibodies directed towards antigenic site A. Thus, a high inherent flexibility of this loop may preclude a conformational restriction strong enough to alter recognition by anti-virus antibodies." @default.
• W1525192669 created "2016-06-24" @default.
• W1525192669 creator A5007990086 @default.
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• W1525192669 date "1993-08-09" @default.
• W1525192669 modified "2023-10-14" @default.
• W1525192669 title "Cyclic disulfide model of the major antigenic site of serotype-C foot-and-mouth disease virus" @default.
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• W1525192669 doi "https://doi.org/10.1016/0014-5793(93)80985-4" @default.
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• W1525192669 hasPublicationYear "1993" @default.
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