Characterization of Recombinant His-Tag Protein Immobilized onto Functionalized Gold Nanoparticles.

ABSTRACT: The recombinant polyhistidine-tagged hemoglobin I ((His)₆-rHbI) from the bivalve Lucina pectinata is an ideal biocomponent for a hydrogen sulfide (H₂S) biosensor due to its high affinity for H₂S. In this work, we immobilized (His)₆-rHbI over a surface modified with gold nanoparticles functionalized with 3-mercaptopropionic acid complexed with nickel ion. The attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) analysis of the modified-gold electrode displays amide I and amide II bands characteristic of a primarily α-helix structure verifying the presence of (His)₆-rHbI on the electrode surface. Also, X-ray photoelectron spectroscopy (XPS) results show a new peak after protein interaction corresponding to nitrogen and a calculated overlayer thickness of 5.3 nm. The

SUBMITTER: Torres-Gonzalez L 

PROVIDER: S-EPMC6308469 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature