NDLI: Self-assembled enzymatic monolayer directly bound to a gold surface: Activity and molecular recognition force spectroscopy studies

Content Provider	PubMed Central
Author	Ditzler, Lindsay R. Sen, Arundhuti Gannon, Michael J. Kohen, Amnon Tivanski, Alexei V.
Abstract	E.coli dihydrofolate reductase (ecDHFR) has one surface cysteine, C152, located opposite and distal to the active site. Here, we show that the enzyme spontaneously assembles on an ultra-flat gold surface as a homogenous, covalently bound monolayer. Surprisingly, the activity of the gold-immobilized ecDHFR as measured by radiographic analysis was found to be similar to that of the free enzyme in solution. Molecular recognition force spectroscopy was used to study the dissociation forces involved in the rupture of AFM probetethered methotrexate (MTX, a tight-binding inhibitor of DHFR) from the gold-immobilized enzyme. Treatment of the ecDHFR monolayer with free MTX diminished the interaction of the functionalized tip with the surface, suggesting that the interaction was indeed active-site specific. These findings demonstrate the viability of a simple and direct enzymatic surface-functionalization without the use of spacers, thus opening the door to further applications in the area of biomacromolecular force spectroscopy.
Related Links	http://dx.doi.org/10.1021/ja205409v
Ending Page	13287
Page Count	4
Starting Page	13284
File Format	PDF
ISSN	00027863
e-ISSN	15205126
Journal	Journal of the American Chemical Society
Issue Number	34
Volume Number	133
Language	English
Publisher Date	2011-08-31
Access Restriction	Open
Subject Keyword	Colloid and Surface Chemistry Biochemistry Chemistry(all) Catalysis Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Colloid and Surface Chemistry Biochemistry Catalysis

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