Herein, we present a greener approach to achieve an ultrasensitive, selective, and viable sensor engineered by amino acids as a recognition layer for simultaneous electrochemical sensing of toxic heavy metals (HMs). Electrochemical techniques like electrochemical impedance spectroscopy (EIS), cyclic voltammetry (CV), and square-wave anodic stripping voltammetry (SWASV) were applied to demonstrate sensing capabilities of the designed analytical tool. The comparative results of different amino acids demonstrate alanine's superior performance with a well-resolved and enhanced current signal for target metal ions due to strong complexation of its functional moieties. The working conditions for alanine-modified GCE were optimized by investigating the effect of alanine concentration, different supporting electrolytes, pH values, accumulation potentials, and time. The limits of detection for Zn, Cd, Cu, and Hg were found to be 8.92, 5.77, 3.01, and 5.89 pM, respectively. The alanine-modified electrode revealed absolute discrimination ability, stability, and ultrasensitivity toward metal ions even in the presence of multifold interfering species. Likewise, greener modifier-designed electrodes possessed remarkable electrocatalytic activity, cost affordability, reproducibility, and applicability for picomolar level detection of HM ions in real water sample matrixes. Theoretical calculations for the HM-amino acid interaction also support a significantly improved mediator role of the alanine modifier that is consistent with the experimental findings.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933785PMC
http://dx.doi.org/10.1021/acsomega.9b03189DOI Listing

Publication Analysis

Top Keywords

amino acids
8
metal ions
8
amino acid-fabricated
4
acid-fabricated glassy
4
glassy carbon
4
carbon electrode
4
electrode efficient
4
efficient simultaneous
4
simultaneous sensing
4
sensing zincii
4

Similar Publications

Norepinephrine in vertebrates and its invertebrate analog, octopamine, regulate the activity of neural circuits. We find that, when hungry, larvae switch activity in type II octopaminergic motor neurons (MNs) to high-frequency bursts, which coincide with locomotion-driving bursts in type I glutamatergic MNs that converge on the same muscles. Optical quantal analysis across hundreds of synapses simultaneously reveals that octopamine potentiates glutamate release by tonic type Ib MNs, but not phasic type Is MNs, and occurs via the G-coupled octopamine receptor (OAMB).

View Article and Find Full Text PDF

Dysregulation of GABAergic inhibition is associated with pathological pain. Consequently, enhancement of GABAergic transmission represents a potential analgesic strategy. However, therapeutic potential of current GABA agonists and modulators is limited by unwanted side effects.

View Article and Find Full Text PDF

The homo-dodecameric ring-shaped RNA binding attenuation protein (TRAP) from binds up to twelve tryptophan ligands (Trp) and becomes activated to bind a specific sequence in the 5' leader region of the operon mRNA, thereby downregulating biosynthesis of Trp. Thermodynamic measurements of Trp binding have revealed a range of cooperative behavior for different TRAP variants, even if the averaged apparent affinities for Trp have been found to be similar. Proximity between the ligand binding sites, and the ligand-coupled disorder-to-order transition has implicated nearest-neighbor interactions in cooperativity.

View Article and Find Full Text PDF

A single-component flavin-dependent halogenase, AetF, has emerged as an attractive biocatalyst for catalyzing halogenation. However, its flavin chemistry remains unexplored and cannot be predicted due to its uniqueness in sequence and structure compared to other flavin-dependent monooxygenases. Here, we investigated the flavin reactions of AetF using transient kinetics.

View Article and Find Full Text PDF

With the advancement of genetic code expansion, the field is progressing towards incorporating multiple non-canonical amino acids (ncAAs). The specificity of aminoacyl-tRNA synthetases (aaRSs) towards ncAAs is a critical factor, as engineered aaRSs frequently show polyspecificity, complicating the precise incorporation of multiple ncAAs. To address this challenge, predicting binding affinity can be beneficial.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!