ArticleACS omega2018
Robust Surface Plasmon Resonance Chips for Repetitive and Accurate Analysis of Lignin-Peptide Interactions.
Article in ACS omega, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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Who cites it
2 citing papers in PubMed, 9 citations in OpenAlex.
- Strategy of Dimercaptothiol as Self-assembled Monolayers Enhance the Sensitivity of SPR Immunosensor for Detection of Salbutamol.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021Article
- Non-productive binding of cellobiohydrolase i investigated by surface plasmon resonance spectroscopy.Cellulose (London, England) · 2021Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed novel surface plasmon resonance (SPR) sensor chips whose surfaces bear newly synthesized functional self-assembled monolayer (SAM) anchoring lignin through covalent chemical bonds. The SPR sensor chips are remarkably robust and suitable for repetitive and accurate measurement of noncovalent lignin-peptide interactions, which is of significant interest in the chemical or biochemical conversion of renewable woody biomass to valuable chemical feedstocks. The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently. The resulting SAMs were characterized using infrared reflection-absorption, Raman, and X-ray photoelectron spectroscopies to confirm covalent immobilization of the lignins to the SAMs via triazole linkages and also to reveal that the SAM formation induces a helical conformation of the ethylene oxide chains. Further, SPR measurements of the noncovalent lignin-peptide interactions using lignin-binding peptides have demonstrated high reproducibility and durability of the prepared lignin-anchored sensor chips.
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Registered trials
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