2014
DOI: 10.1016/j.snb.2014.06.030
|View full text |Cite
|
Sign up to set email alerts
|

Binding and potential-triggered release of l-glutamate with molecularly imprinted polypyrrole in neutral pH solutions

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

2
7
0

Year Published

2015
2015
2022
2022

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 12 publications
(9 citation statements)
references
References 33 publications
2
7
0
Order By: Relevance
“…The mechanism of uptake is similar to the findings of Paul et al. [ 21 ]. They studied uptake and reverse uptake processes using a molecularly imprinted polymer (MIP) and found a relationship between glutamate concentration and voltage pulse on the MIP electrode.…”
Section: Resultssupporting
confidence: 90%
See 1 more Smart Citation
“…The mechanism of uptake is similar to the findings of Paul et al. [ 21 ]. They studied uptake and reverse uptake processes using a molecularly imprinted polymer (MIP) and found a relationship between glutamate concentration and voltage pulse on the MIP electrode.…”
Section: Resultssupporting
confidence: 90%
“…A molecular imprinting method was previously introduced for neurotransmitter uptake into an over-oxidized conducting polymer. However, this method requires pretreatment of polypyrrole, which includes oxidizing and exchanging ions [ 21 , 22 , 23 ]. Therefore, this study proposes an easier uptake method for a neurotransmitter using carbon-based materials.…”
Section: Introductionmentioning
confidence: 99%
“…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%
“…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%