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

Journal of biosciences

Jing Wu¹  Min-Chen Wu¹  Lian-Fen Zhang¹  Jian-Yong Lei¹  Lei Feng¹  Jian Jin1 2¹ 

[1] School of Medicine and Pharmaceutics, Jiangnan University, Wuxi, Jiangsu 214122, China$$

关键词: Inhibitory effect;    integrin 𝛼v𝛽3;    interaction;    phage display;    recombinant ADAM15 disintegrin domain;    target peptide;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

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.

【 授权许可】

Unknown