Abstract
This study investigated a strategy by which antibodies are displayed to engage T cells. A peptide composite containing binding sites was characterized in vitro and explored as an injectable system in vivo. The composite consists of two amphiphilic peptides, AEAEAKAKAEAEAKAK (referred to as "EAK" ) and EAK appended with six consecutive histidines at the C-terminus (" EAKH6" ). Spectroscopic analysis showed the two peptides integrated into a single structure. Prior to combination, conformational analysis revealed that EAKH6 adopts a mixed α-helix/β-strand conformation. In the presence of EAK, EAKH6 exists predominately in β-strand conformation. The composite of EAK-EAKH6 was found to display His-tags, using nickel-bound horseradish peroxidase as a probe. T cell-specific antibodies were found stably displayed on the EAK-EAKH6 assembly using recombinant protein A/G and anti-histidines antibody as an adaptor. When mounted with anti-CD4 antibody, the system was shown to capture CD4. T cells in a mixed population of lymphocytes. Antibodies were concentrated in the subcutaneous space in mice when co-administered with EAK and EAKH6 along with protein A/G and anti-histidines antibody as a solution. We report here the use of amphiphilic peptides to display Ab in vivo, the results indicating that the design can be used as a platform for engaging specific subsets of leukocytes for the purpose of immune modulation.
Original language | English (US) |
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Pages (from-to) | 249-257 |
Number of pages | 9 |
Journal | Biomaterials |
Volume | 32 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2011 |
Keywords
- Amphiphilic peptides
- Clustered antibodies
- Self-assembly material
- T cells
ASJC Scopus subject areas
- Biophysics
- Bioengineering
- Ceramics and Composites
- Biomaterials
- Mechanics of Materials