2015
DOI: 10.1016/j.snb.2015.01.109
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Characterization of caffeine-imprinted polypyrrole by a quartz crystal microbalance and electrochemical impedance spectroscopy

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Cited by 87 publications
(71 citation statements)
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“…The obtained value of Gibbs free energy change is in the same order as that value calculated by other authors [28] and confirmed in our previous works [27]. These values are close to that which are typical for 2-3 hydrogen bounds formation and electrostatic interactions [29,30].…”
Section: Evaluation Of Theophylline Interaction With Mip-ppysupporting
confidence: 91%
See 1 more Smart Citation
“…The obtained value of Gibbs free energy change is in the same order as that value calculated by other authors [28] and confirmed in our previous works [27]. These values are close to that which are typical for 2-3 hydrogen bounds formation and electrostatic interactions [29,30].…”
Section: Evaluation Of Theophylline Interaction With Mip-ppysupporting
confidence: 91%
“…where the K D 0 = K D /c, in this case the c is the concentration of theophylline; Therefore, the K D 0 is the value, which is calculated for standard reference concentration of 1 M [27].…”
Section: Evaluation Of Theophylline Interaction With Mip-ppymentioning
confidence: 99%
“…Polypyrrole (Ppy), the one of conducting polymers, has been widely used for sensor applications. During the formation of Ppy layers can be modified by molecular imprints and in such way molecularly imprinted Ppy can be formed (MIP‐Ppy), which contains molecularly imprinted sites, which are complementary and selective for imprinted target molecules. The most efficient formation of MIP‐Ppy can be based on electrochemical polymerization of the pyrrole monomer in the presence of target molecules .…”
Section: Introductionmentioning
confidence: 99%
“…In addition, comparison of the dissociation constants, Kds, derived from binding kinetics might shed light on binding affinity between IgG and the synthesized IgG‐MIPs . The calculated Kd values (3.1nM, 4.8nM, and 5.0nM for IgG‐MI‐PmPD, IgG‐MI‐PDA, and IgG‐MI‐PEDOT, respectively) were in consistence with the conclusions above, demonstrating somewhat higher binding affinity of IgG to IgG‐MI‐PmPD.…”
Section: Resultsmentioning
confidence: 99%