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quartz crystal microbalance in biomolecular recognition
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Figure 14.6. Synthesis of solid-phase peptide with a thio-end group.
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Figure 14.7. A simulated molecular architecture of the A : C mixed SAM sensor surface.
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(A : C and B : C) are believed to have the characteristics of self-assembly, monolayering, and minimal nonspeci c binding. While the B : C surface was used as the control, the A : C surface could bind vancomycin and gave signals in QCM. Figure 14.7 simulates the molecular architecture of surfaces.
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Binding Measurements of Vancomycin to the Immobilized Peptides on QCM Sensor Surfaces Three QCM experiments based on vancomycin peptide interactions were conducted. First, vancomycin was used as the sample to inject to the A : C mixed monolayer surface and PBS was used as the running buffer (pH 7.3). The second experiment was carried out under a condition similar to the rst experiment, but the value of the pH was changed to 2.1. The third experiment used the B : C surface and PBS running buffer (pH 7.3) for vancomycin peptide binding study. Since second and third QCM experiments were employed as the control for the rst measurement, as expected, vancomycin could only be correctly associated with the d-Ala-d-Ala containing peptide on the A : C surface at the physiological pH (Figure 14.8). Using QCM, we could not only qualitatively determine the speci city of individual binding interaction but also quantitatively measure their binding constants. Figure 14.9 shows a representative QCM frequency shift as a
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Gly-Gly- DAla-DAla-OH O
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[vancomycin] = 120 mM in phosphate buffer at pH 2.1
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-30 -40 -50 -60 0 500 1000 1500
Time (s) S
Gly-Gly-LAla-LAla-OH O
[vancomycin] = 120 mM in PBS buffer at pH 7.3
Gly-Gly-DAla-DAla-OH O
[vancomycin] = 120 mM in PBS buffer at pH 7.3
Figure 14.8. Use of QCM to determine binding speci city of vancomycin peptide interactions.
quartz crystal microbalance in biomolecular recognition
100 80 60 DADA pH7.2 DADA pH2.1 LALA pH7.2
-D F (Hz)
40 20 0 -20 0 50 100 Concentration (mM) 150
Figure 14.9. Frequency shift increases in QCM measurements along with increases of vancomycin concentration in the binding interaction study.
function of the injected vancomycin concentration under equilibrium conditions in the vancomycin peptide binding system. It was found that on the A : C surface at pH 7.3, the frequency shift increased with each increase of vancomycin concentration. In the A : C mixed monolayer on the QCM sensor surface at pH2.1, the frequency changed insigni cantly under the various vancomycin concentrations. This result demonstrated that in vancomycin peptide interactions the binding must take place at physiological pHs. As expected for the B : C sensor surface at pH 7.3, the shifts in QCM frequency provided no evidence of difference for the various vancomycin concentrations, implying that vancomycin does not bind with the L-Ala-LAla containing peptide. All of the above-mentioned results clearly show that given the QCM conditions of our experiments, the nonspeci c interactions between vancomycin and immobilized peptides are minimal, if not entirely avoided. The frequency shifts of the QCM, when detected experimentally, seem to result from speci c binding. The results also show that without optimal conditions for binding (i.e., pH 2.1, instead of pH 7.3), no speci c recognition occurs between vancomycin and the peptides. Quantitative Dissociation Constant Measurements The measurement of dissociation constants greatly helps the understanding of the mechanisms involved in biomolecular recognition. The dissocia-
molecular recognition
0.2 0.15 DF 1 [vanco] 0.05 0 0 0.2 0.4 0.6 DF Fma x 0.8 1 0.1
Fma x
Figure 14.10. Scatchard analysis of the binding interaction between vancomycin and a D-AlaD-Ala containing peptide (ligand A) measured by QCM.
tion constant Kd between vancomycin and a d-Ala d-Ala containing peptide can be calculated using the equation (the Scatchard equation) L + Vanco DF 1 Fmax [Vanco] Ka Kd =
[L Vanco]
1 DF 1. Kd Fmax (14.3)
The slope of the curve in the plot of DF/(Fmax [Vanco]) versus DF/Fmax gives the binding constant of a biochemical system.69 From (14.3), Kd can be readily obtained. The binding data presented in Figure 14.9 can be used for Scatchard analysis to calculate the corresponding dissociation constant. Figure 14.10 shows the result of such Scatchard analysis. The Kd for vancomycin binding with the peptide was 5.5 mM, which is correlated well with the value reported in the literature. 14.2.4. QCM for High-Throughput Screening of Compound Libraries
Combinatorial chemistry has been a useful tool for new drug development. Many researchers in the past have applied and utilized this technology for massive screening of the active compound from compound libraries in a relatively short time in order to nd potential drug candidates. The same approach has been used to nd the best substrates of enzymes. In successful combinatorial chemistry research, the development of high-throughput