ANTIBODY RECOGNITION OF PEPTIDE SEQUENCES FROM THE CELL-CELL ADHESIONPROTEINS - N-CADHERIN AND E-CADHERIN

Intercellular functions present a formidable challenge for the paracel lular delivery of drugs. Cadherins are calcium-dependent cell-cell adh esion. molecules, which are responsible for the formation and regulati on of these junctions. Anti-E-cadherin monoclonal antibody can bind to E-cadherin (uvomorulin) and inhibit cell-cell adhesion through the in hibition of cadherin-cadherin interactions. The objective of this stud y was to utilize this monoclonal anti-E-cadherin antibody to map the e xtra cellular domains of E- and N-cadherin. This was accomplished by u sing two different enzyme-linked immunosorbent assays (ELISAs), a regu lar indirect ELISA and an immobilized-peptide ELISA. Two peptides from each extracellular domain were recognized by this anti-E-cadherin ant ibody. By mapping the extracellular domains of cadherins, peptides tha t have discrete roles in cell-cell adhesion call be identified. This w ill aid in the design of synthetic peptides that can modulate intercel lular junctions to improve drug delivery.