Structure-activity studies of peptides from the "hot-spot" region of human CD2 protein: Development of peptides for immunomodulation

Jining Liu, Jinfa Ying, Vincent T.K. Chow, Victor J. Hruby, Seetharama D. Satyanarayanajois

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


CD2 is a cell surface protein belonging to the immunoglobulin superfamily (IgSF) that plays a key role in mediating adhesion between human T-lymphocytes and target cells. The interaction between cell-adhesion molecules CD2 and CD58 is critical for immune response. Modulation or inhibition of these interactions has been shown to be therapeutically useful. Synthetic 12-mer linear and cyclic peptides and cyclic hexapeptides from the β-turn and β-strand region (hot spot) of human CD2 protein were designed to modulate CD2-CD58 interaction. The 12-amino acid synthetic cyclic peptides effectively blocked the interaction between CD2 and CD58 proteins as demonstrated by E-rosetting and heterotypic adhesion assays. NMR and molecular modeling studies indicated that these cyclic peptides exhibit β-turn structure in solution and closely mimic the β-turn structure of the surface epitopes of CD2 protein. The designed cyclic peptides with β-turn structure have the ability to modulate CD2-CD58 interaction.

Original languageEnglish (US)
Pages (from-to)6236-6249
Number of pages14
JournalJournal of Medicinal Chemistry
Issue number20
StatePublished - Oct 6 2005

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery


Dive into the research topics of 'Structure-activity studies of peptides from the "hot-spot" region of human CD2 protein: Development of peptides for immunomodulation'. Together they form a unique fingerprint.

Cite this