Abstract
In order to improve the immunotherapeutical potential of H-Cys-Leu-Gly-Gly-Leu-Leu-Thr-Met-Val-OH (CLG) peptide, an Epstein-Barr virus (EBV) subdominant epitope derived from the membrane protein LMP2, we have synthesized and tested CLG analogues containing cis- and/or trans-4-aminocyclohexanecarboxylic acid (ACCA) replacing Gly-Gly and/or Thr-Met dipeptide units. All pseudopeptides were tested for metabolic stability and for their capacity to bind HLA-A2 molecules and to sensitize target cells to lysis. All new compounds exhibited higher enzymatic resistance compared to the original CLG and some trans-ACCA-derivatives were able to associate HLA-A2 and to efficiently stimulate CTL responses directed against the CLG natural epitope.
Original language | English (US) |
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Pages (from-to) | 3061-3066 |
Number of pages | 6 |
Journal | Bioorganic and Medicinal Chemistry |
Volume | 10 |
Issue number | 9 |
DOIs | |
State | Published - 2002 |
Bibliographical note
Funding Information:Financial support of this work by University of Ferrara, by Ministero dell'Università e della Ricerca Scientifica e Tecnologica (MURST) and by Istituto Superiore di Sanità (AIDS project) is gratefully acknowledged.