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Secondary structure-improved bioaffinity correlation in elongated and modified synthetic epitope peptides from p24 HIV-1 core protein |
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| Authors: | Georgina Tonarelli Javier Lottersberger Jorge L. Salvetti Saul Jacchieri Rosemeire A. Silva-Lucca Leila M. Beltramini |
| Affiliation: | (1) Departamento Química. Orgánica, Facultad de Bioquímica y Cs. Biológicas, UNL, Ciudad Universitaria, C.C. 242, 3000 Santa Fe, Argentina;(2) Fundação Antônio Prudente, Centro de Pesquisas, Rua Prof Antônio Prudente 211, São Paulo, SP 01509-090, Brazil;(3) Departamento de Física e Informática, Grupo de Biofísica Molecular, Instituto de Física de São Carlos, São Paulo, Brazil |
| Abstract: | In order to study the correlation between secondarystructure and bioaffinity of long and modified sequences ofp24 protein from HIV-1, three peptides containing the minimalsize epitope from region 208-217 (EAAEWDRVHP) were prepared.It was found that peptide p24-1n, an elongated nativesequence, has the lowest KD and a predominant -helix structure in the presence of trifluoroethanol. Three peptides containing another epitope from region 293-302 (FRDYVDRFK)were also synthesized. We have observed that modifications onthe native sequence p24-2n (region 287-308) increased the -helix content and this was correlated with an improvement of the recognition by antibodies in ELISA. |
| Keywords: | bioaffinity circular dichroism conformation immunoassays molecular modelling synthetic peptides |
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