Biomedical Engineering Reference
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Fig. 9 Glucose competition curves showing the normalized DBA fluorescence intensity versus
glucose concentration for DBA 1, DBA 2, and DBA 3 in physiological buffer at neutral pH on an
iDIOL 3 surface (a). Binding constants, in the Keq interaction graph, for DBA 1, 2, and/or 3:
glucose and DBA 1, 2, and/or 3:diol combinations were correlated with the glucose response
curves of each DBA:iDIOL system (b)
a
b
F
OH
OH
B
B
H
OH
H
OH
F
c
d
OH
OH
F
OH
HO
OH
B
H
OH
O
HO
C
F
NH
Fig. 10 Structures of DBA 1 (a), DBA 2 (b), DBA 3 (c), and iDIOL 3 (d) evaluated for binding
performance in a glucose competition binding assay
surface. These glucose competition curves illustrate that the DBA responded, as
would be expected from their DBA:diol Keq values, to changing levels of glucose
with significant diversity relative to the iDIOLs. Previously determined binding
constants for DBA:glucose and DBA:diol combinations were correlated with the
glucose response curves of each DBA:iDIOL system (Fig. 12b ). Keq vlaues for the
diols corresponding to iDIOL 1 and iDIOL 2 are above the DBA:glucose versus
DBA:diol 1:1 line, indicating that the DBA has less affinity for glucose than either the
 
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