Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768014 | Biochemical and Biophysical Research Communications | 2005 | 4 Pages |
Abstract
Four chimeric synthetic peptides (Q5, Q6, Q7â, and Q8â), incorporating immunodominant epitopes of the core p19 (105-124Â a.a.) and envelope gp46 proteins (175-205Â a.a.), of HTLV-I were obtained. Also, two gp46 monomeric peptides M4 and M5â (Ser at position 192) were synthesized. The analysis of the influence of the peptide lengths and the proline to serine substitution on the chimeric and monomeric peptides' antigenicity, with regard to the chimeric peptides Q1, Q2, Q3â, and Q4â, reported previously, for HTLV-I was carried out. The peptides' antigenicity was evaluated in an ultramicroenzyme-linked immunosorbent assay (UMELISA) using sera of HTLV-I/II. The peptides' antigenicity was affected appreciably by the change of the peptide length and amino acid substitutions into the immunodominant sequence of gp46 peptide.
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Authors
Milenen Hernández Marin, Chryslaine RodrÃguez-Tanty, David Higginson-Clarke, Yadaris Márquez Bocalandro, Lilliam Pozo Peña,