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

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.

SUBMITTER: Wang SH

PROVIDER: S-EPMC5063806 | biostudies-other | 2016 Jun

REPOSITORIES: biostudies-other

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

Wang Sheng-Hung SH Yu John J

Data in brief 20160504

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 n ...[more]

PMID: 27761511

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Project description:Biocatalysis is a useful strategy for sustainable green synthesis of fine chemicals due to its high catalytic rate, reaction specificity, and operation under ambient conditions. Addressable immobilization of enzymes onto solid supports for one-pot multistep biocatalysis, however, remains a major challenge. In natural pathways, enzymes are spatially coupled to prevent side reactions, eradicate inhibitory products, and channel metabolites sequentially from one enzyme to another. Construction of a modular immobilization platform enabling spatially directed assembly of multiple biocatalysts would, therefore, not only allow the development of high-efficiency bioreactors but also provide novel synthetic routes for chemical synthesis. In this study, we developed a modular cascade flow reactor using a generalizable solid-binding peptide-directed immobilization strategy that allows selective immobilization of fusion enzymes on anodic aluminum oxide (AAO) monoliths with high positional precision. Here, the lactate dehydrogenase and formate dehydrogenase enzymes were fused with substrate-specific peptides to facilitate their self-immobilization through the membrane channels in cascade geometry. Using this cascade model, two-step biocatalytic production of l-lactate is demonstrated with concomitant regeneration of soluble nicotinamide adenine dinucleotide (NADH). Both fusion enzymes retained their catalytic activity upon immobilization, suggesting their optimal display on the support surface. The 85% cascading reaction efficiency was achieved at a flow rate that kinetically matches the residence time of the slowest enzyme. In addition, 84% of initial catalytic activity was preserved after 10 days of continuous operation at room temperature. The peptide-directed modular approach described herein is a highly effective strategy to control surface orientation, spatial localization, and loading of multiple enzymes on solid supports. The implications of this work provide insight for the single-step construction of high-power cascadic devices by enabling co-expression, purification, and immobilization of a variety of engineered fusion enzymes on patterned surfaces.

Dataset Information

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

Publications

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

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