Person:
Moreno Guzmán, María

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First Name
María
Last Name
Moreno Guzmán
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Farmacia
Department
Química en Ciencias Farmacéuticas
Area
Química Analítica
Identifiers
UCM identifierORCIDScopus Author IDWeb of Science ResearcherIDDialnet IDGoogle Scholar ID

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Now showing 1 - 2 of 2
  • Item
    Aligned copper nanowires as a cut-and-paste exclusive electrochemical transducer for free-enzyme highly selective quantification of intracellular hydrogen peroxide in cisplatin-treated cells
    (Biosensors and Bioelectronics, 2017) García-Carmona, Laura; Moreno Guzmán, María; Martín, Aida; Benito Martínez, Selma; Fernández-Martínez, Ana B.; González, María Cristina; Lucio-Cazaña, Javier; Escarpa, Alberto
    The role and reliable quantification of intracellular hydrogen peroxide during cancer therapy constitutes an unexplored and fascinating application. In this work, we report the fabrication of vertically aligned copper nanowires (v-CuNWs) using electrosynthesis on templates, and their application as a cut-and-paste exclusive and flexible electrochemical transducer. This easily adaptable electrodic platform is demonstrated for a fast, simple and free-enzyme selective quantification of intracellular hydrogen peroxide in Cisplatin-treated human renal HK-2 cells. The v-CuNWs sensor was compared with an HRP-enzyme-based biosensor showing excellent correlation and indicates the good selectivity and analytical performance of the v-CuNWs. This sensing approach opens novel avenues for monitoring cell death processes and shows the potential of H2O2 as a cellular damage biomarker, with a clear potency for further developments for in vitro diagnosis and its implication in cancer therapy.
  • Item
    Class enzyme-based motors for “on the fly” enantiomer analysis of amino acids
    (Biosensors and Bioelectronics, 2017) García-Carmona, Laura; Moreno Guzmán, María; González, María Cristina; Escarpa, Alberto
    Here, two class-enzyme motors are properly designed allowing the rapid dispersion of the class-enzyme D-amino acid oxidase (DAO) and L-amino acid oxidase (LAO) for selective “on the fly” biodetection of D and L-amino acids (AAs), respectively. The efficient movement together with the continuous release of fresh class-enzyme leads to a greatly accelerated enzymatic reaction processes without the need of external stirring or chemical and physical attachment of the enzyme. Ultra-fast detection (<2 min) and accurate quantifications of L-phenylalanine (L-Phe) in plasma and whole-blood newborns samples diagnosed with Phenylketonuria and total D-AAs in Vibrio cholera cultures are pioneer illustrated as relevant examples of each enantiomer determination. These results opens clearly novel avenues in biosensing for fast screening diagnostics, decentralized monitoring and design of future points of care.