Alfredo Sánchez

Dr. Alfredo Sánchez

Complutense University. Chemistry Faculty. Plaza de las Ciencias s/n 28040 Madrid (SPAIN)
orcid

Research Focus & Metrics

Academic Career Length

20Years (2007-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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10 March 2016 in RSC Advances
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Journal Article
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ASAlfredo Sánchez
Alfredo Sánchez
JCJenniffer Cruz
Jenniffer Cruz
NRNazzoly Rueda
Nazzoly Rueda
José Cleiton Sousa dos SantosJosé Cleiton Sousa dos Santos
José Cleiton Sousa dos Santos
RTRodrigo Torres
Rodrigo Torres
Roberto Fernandez-LafuenteRoberto Fernandez-Lafuente
Roberto Fernandez-Lafuente
Bovine trypsin immobilized on glyoxyl agarose and submitted to different inactivation conditions produce different conformations.

30 May 2017 in Nature Communications
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Journal Article
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ALAntoni Llopis-Lorente
Antoni Llopis-Lorente
PDPaula Díez
Paula Díez
ASAlfredo Sánchez
Alfredo Sánchez
MMM. Dolores Marcos
M. Dolores Marcos
FSFélix Sancenón
Félix Sancenón
RMRamón Martínez-Máñez
Ramón Martínez-Máñez
‘Communication’ between abiotic nanoscale chemical systems is an almost-unexplored field with enormous potential. Here we show the design and preparation of a chemical communication system based on enzyme-powered Janus nanoparticles, which mimics an interactive model of communication. Cargo delivery from one nanoparticle is governed by the biunivocal communication with another nanoparticle, which involves two enzymatic processes and the interchange of chemical messengers. The conceptual idea of establishing communication between nanodevices opens the opportunity to develop complex nanoscale systems capable of sharing information and cooperating.

6 June 2014 in Journal of the American Chemical Society
Verified
Journal Article
Closed access
PDPaula Díez
Paula Díez
ASAlfredo Sánchez
Alfredo Sánchez
MCMaria Gamella Carballo
Maria Gamella Carballo
PMPaloma Martínez-Ruíz
Paloma Martínez-Ruíz
EAElena Aznar
Elena Aznar
José Manuel PingarrónJosé Manuel Pingarrón
José Manuel Pingarrón

1 September 2007 in Journal of Colloid and Interface Science
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Journal Article
Closed access
DPDamián Pérez-Quintanilla
Damián Pérez-Quintanilla
ASAlfredo Sánchez
Alfredo Sánchez
IHIsabel Del Hierro
Isabel Del Hierro
MFMariano Fajardo
Mariano Fajardo
Isabel SierraIsabel Sierra
Isabel Sierra

14 April 2015 in RSC Advances
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Journal Article
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José Cleiton Sousa dos SantosJosé Cleiton Sousa dos Santos
José Cleiton Sousa dos Santos
NRNazzoly Rueda
Nazzoly Rueda
ASAlfredo Sánchez
Alfredo Sánchez
Reynaldo Villalonga SantanaReynaldo Villalonga Santana
Reynaldo Villalonga Santana
Luciana Rocha Barros GoncalvesLuciana Rocha Barros Goncalves
Luciana Rocha Barros Goncalves
Roberto Fernandez-LafuenteRoberto Fernandez-Lafuente
Roberto Fernandez-Lafuente
The lipase B from C. antarctica (CALB) has been immobilized on divinylsulfone (DVS) activated agarose beads under different conditions (pH 5–10). In the presence of 0.3% Triton X-100, the immobilization rate was rapid at pH 10 and the slowest one was at pH 5. Incubation at pH 10 for 72 h of the immobilized enzymes before blocking of the support with ethylenediamine permitted improvement of the enzyme stability. Enzyme features (activity, stability, specificity versus different substrates, effect of the pH on enzyme properties) were quite different on the different CALB preparations, suggesting the different orientation of the enzyme. The alkaline incubation produced an increase in enzyme activity with some substrates, and some of the DVS-CALB preparations exhibited a higher specific activity than the octyl-preparations. The indirect fluorescence spectrum of the different immobilized preparations confirmed that different structures of the CALB molecules were generated after immobilization.

1 February 2018 in Sensors and Actuators B: Chemical
Verified
Journal Article
Closed access
WAWicem Argoubi
Wicem Argoubi
ASAlfredo Sánchez
Alfredo Sánchez
CPConcepción Parrado
Concepción Parrado
NRNoureddine Raouafi
Noureddine Raouafi
RVReynaldo Villalonga
Reynaldo Villalonga