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• W2014927241 abstract "The binding of Cry1Ac, an insecticidal protein of Bacillus thuringiensis, to a brush border membrane (BBM) isolated from midguts of the diamondback moth Plutella xylostella was examined by surface plasmon resonance (SPR)-based biosensor. BBM was mixed with 1,3-ditetradecylglycero-2-phosphocholine (PC14), a neutral charged artificial lipid, and was reconstructed to a monolayer on a hydrophobic chip for the biosensor. The binding of Cry1Ac to the reconstructed monolayer was analyzed by a two-state binding model, and it was shown that Cry1Ac bound to the monolayer in the first step with an affinity constant (K(1)) of 508 nM, followed by the second uni-molecular step with an equilibrium constant (K(2)) of 0.472. The overall affinity constant K(d) was determined to be 240 nM. The binding was markedly inhibited by N-acetyl-D-galactosamine (K(i)=8 mM). The monolayer was shown to retain a high affinity to Cry1Ac, providing an insect-free system for rapid and large-scale screening of B. thuringiensis insecticidal proteins by the SPR-based biosensor technology." @default.
• W2014927241 created "2016-06-24" @default.
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• W2014927241 date "2001-02-01" @default.
• W2014927241 modified "2023-10-16" @default.
• W2014927241 title "Screening of the Bacillus thuringiensis Cry1Ac δ-endotoxin on the artificial phospholipid monolayer incorporated with brush border membrane vesicles of Plutella xylostella by optical biosensor technology" @default.
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• W2014927241 doi "https://doi.org/10.1016/s0165-022x(00)00134-2" @default.
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