Data for peptide-binding assay with oriented immobilization of GRP78 in Biacore

Sheng-Hung Wang; John Yu

doi:10.1016/j.dib.2016.04.064

Data for peptide-binding assay with oriented immobilization of GRP78 in Biacore

Data Brief. 2016 May 4:7:1696-1699. doi: 10.1016/j.dib.2016.04.064. eCollection 2016 Jun.

Authors

Sheng-Hung Wang¹, John Yu¹

Affiliation

¹ Institute of Stem Cell and Translational Cancer Research, Chang Gung Memorial Hospital at Linkou, and Chang Gung University, Taoyuan 333, Taiwan.

Abstract

To develop peptide-conjugated liposomes for cancer imaging and therapy, the label-free surface plasmon resonance (SPR) biosensor (Biacore™) is a practical and also preferred strategy to examine protein-peptide interaction. A new Biacore protocol with "oriented immobilization" for peptide-binding assay, which overcomes the drawbacks of conventional protocols, was presented in this data article. These results were complementary to the research article Wang at al., [1], which reported a series of new cancer-targeting peptides found with HotLig software (Wang et al., 2013) [2], and this newly developed Biacore protocol.

Keywords: Biacore; EDC, 1-Ethyl-3-(3-dimethylaminopropyl)-carbodiimide; GRP78; L-peptide; NHS, N-Hydroxysuccinimide; NTA, nitrilotriacetic-acid; RLLDTNRPLLPY; SPR, surface plasmon resonance; Surface plasmon resonance.