STRUCTURE-ACTIVITY STUDIES OF CTL INHIBITORY PEPTIDES DERIVED FROM HLA CLASS-I MOLECULES

Authors
SCHWARTZ EJ GOLDBERG J CLAYBERGER C KRENSKY AM GRIFFIN JH
Citation
Ej. Schwartz et al., STRUCTURE-ACTIVITY STUDIES OF CTL INHIBITORY PEPTIDES DERIVED FROM HLA CLASS-I MOLECULES, Bioorganic & medicinal chemistry letters, 7(1), 1997, pp. 37-40
Citations number
14
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
7
Issue
1
Year of publication
1997
Pages
37 - 40
Database
ISI
SICI code
0960-894X(1997)7:1<37:SSOCIP>2.0.ZU;2-V
Abstract
A series of dimeric peptides derived from a conserved HLA Class I hexa peptide sequence have been synthesized and tested for their ability to inhibit T cell-mediated lysis and to disrupt membranes. Structure-act ivity studies of the C-N/N-C dimer show that activity is especially se nsitive to substitution of isoleucine residues. The results further de fine and delimit the basis for activity by HLA-derived peptides. Copyr ight (C) 1996 Elsevier Science Ltd