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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.7b02919
|2 doi
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|a pubmed24n1590.xml
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|a (DE-627)NLM278936229
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|a (NLM)29228779
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Baveghems, Clive L
|e verfasserin
|4 aut
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|a Tuning Enzyme/α-Zr(IV) Phosphate Nanoplate Interactions via Chemical Modification of Glucose Oxidase
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 11.09.2018
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|a Date Revised 04.11.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Using glucose oxidase (GOx) and α-Zr(IV) phosphate nanoplates (α-ZrP) as a model system, a generally applicable approach to control enzyme-solid interactions via chemical modification of amino acid side chains of the enzyme is demonstrated. Net charge on GOx was systematically tuned by appending different amounts of polyamine to the protein surface to produce chemically modified GOx(n), where n is the net charge on the enzyme after the modification and ranged from -62 to +95 electrostatic units in the system. The binding of GOx(n) with α-ZrP nanosheets was studied by isothermal titration calorimetry (ITC) as well as by surface plasmon resonance (SPR) spectroscopy. Pristine GOx showed no affinity for the α-ZrP nanosheets, but GOx(n) where n ≥ -20 showed binding affinities exceeding (2.1 ± 0.6) × 106 M-1, resulting from the charge modification of the enzyme. A plot of GOx(n) charge vs Gibbs free energy of binding (ΔG) for n = +20 to n = +65 indicated an overall increase in favorable interaction between GOx(n) and α-ZrP nanosheets. However, ΔG is less dependent on the net charge for n > +45, as evidenced by the decrease in the slope as charge increased further. All modified enzyme samples and enzyme/α-ZrP complexes retained a significant amount of folding structure (examined by circular dichroism) as well as enzymatic activities. Thus, strong control over enzyme-nanosheet interactions via modulating the net charge of enzymes may find potential applications in biosensing and biocatalysis
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Enzymes, Immobilized
|2 NLM
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|a zirconium phosphate
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|a 13765-95-2
|2 NLM
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|a Zirconium
|2 NLM
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|a C6V6S92N3C
|2 NLM
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|a Glucose Oxidase
|2 NLM
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|a EC 1.1.3.4
|2 NLM
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|a Ethyldimethylaminopropyl Carbodiimide
|2 NLM
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|a RJ5OZG6I4A
|2 NLM
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|a Trientine
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|a SJ76Y07H5F
|2 NLM
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1 |
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|a Anuganti, Murali
|e verfasserin
|4 aut
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1 |
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|a Pattammattel, Ajith
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lin, Yao
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kumar, Challa V
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 34(2018), 1 vom: 09. Jan., Seite 480-491
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:34
|g year:2018
|g number:1
|g day:09
|g month:01
|g pages:480-491
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|u http://dx.doi.org/10.1021/acs.langmuir.7b02919
|3 Volltext
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|d 34
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|b 09
|c 01
|h 480-491
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