Identification of binding peptides of the ADAM15 disintegrin domain using phage display

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ADAM15 plays an important role in tumour development by interacting with integrins. In this study, we investigated the target peptides of the ADAM15 disintegrin domain. First, we successfully produced the recombinant human ADAM15 disintegrin domain (RADD) that could inhibit melanoma cell adhesion by using Escherichia coli. Second, four specific binding peptides (peptides A, B, C, and D) were selected using a phage display 12-mer peptide library. The screening protocol involved 4 rounds of positive panning on RADD and 2 rounds of subtractive selection with streptavidin. By using the BLAST software and a relevant protein database, integrin αvβ3 was found to be homologous to peptide A. Synthetic peptide A had a highly inhibitory effect on RADD-integrin αvβ3 binding. The results demonstrate the potential application of short peptides for disrupting high-affinity ADAM-integrin interactions.

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