Building and Testing of a MUHEG Capped Quantum Dot Lead Biosensor Specific Against Mercury Quenching
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Authors
Gerlach, Gary F., II
Issue Date
2008
Type
Presentation
Language
en_US
Keywords
Alternative Title
Abstract
Biosensors utilize biological and physicochemical
detector component to detect an analyte.
A metalloprotein backbone reporter element was elicited
as the biological component to the biosensor. The lead
binding metalloprotein (PbBP) used is of the hinge motion
binding protein (HMBP) family. Hinge motion binding
proteins undergo a conformational change in protein
structure, PbBP specifically brings the amino and carboxyl
terminus of the protein into close proximity.
Physicochemical detection is produced with an electron
accepting quantum dot and its complimentary electron donor
a ruthenium(II) metal complex.
Physical attributes to the biosensor provide the
mechanism for analyte detection. The change in protein
structure allows the n-terminus positioned ruthenium(II)
metal complex to donate an electron to the c-terminus
positioned quantum dot (QD). The transferred electron
ceases the QD’s fluorescence, this is termed a “quench.”
In previous experiments lead biosensors have proven
effective at detecting lead concentrations at low levels
(5 μm). However the biosensor finds lacking in its
specificity. With experiments conducted in the presence of
mercury(II) a 90 % quench was registered. A
metallothionein (MT) capping group was distinguished as
problematic for its high cysteine count.
In aim to rectify the lead biosensor’s quench and provide
better specificity for it a (1-Mercaptoundec-11-
yl)hexa(ethylene glycol), MUHEG, capping group was
synthesized and replaced the MT capping group on the QDs
Description
Citation
Publisher
Kalamazoo, Mich. : Kalamazoo College.
License
U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.