000165382 001__ 165382
000165382 005__ 20260107201858.0
000165382 0247_ $$2doi$$a10.1039/D5NR03119B
000165382 0248_ $$2sideral$$a147030
000165382 037__ $$aART-2025-147030
000165382 041__ $$aeng
000165382 100__ $$0(orcid)0000-0003-3459-8605$$aMarcuello, Carlos
000165382 245__ $$aOn-chip EPR spectrometry of metalloproteins using superconducting lumped element resonators
000165382 260__ $$c2025
000165382 5060_ $$aAccess copy available to the general public$$fUnrestricted
000165382 5203_ $$aWe report electron paramagnetic resonance experiments performed on myoglobin hemeproteins using a chip hosting 6 superconducting lumped element resonators with resonance frequencies between 1.94 and 2.11 GHz. Successive layers of myoglobin were deposited onto the inductors of four of them using dip-pen nanolithography, a technique based on atomic force microscopy. A combination of atomic force and confocal microscopies estimated the number of protein molecules in each deposit, which ranges from 8.6 × 10^11 (one dip-pen layer) to 3.33 × 10^12 (four dip-pen layers). Two reference bulk samples were pipetted from the same solution onto the remaining two resonators. The microwave transmission of the device, measured at 11 mK, shows evidence of the coupling of protein spins to the photon excitations of all resonators. In particular, the resonance broadening measured as a function of magnetic field provides the spin resonance absorption spectrum. The analysis suggests that proteins tend to self-orient on the chip. It also allows estimating the single spin to single photon coupling strength, which is around 9 Hz. This high coupling value suggests that dip-pen nanolithography gives rise to a close to optimum interface between the molecules and the chip surface. The developed methodology combines an increase in sensitivity of at least three orders of magnitude with the ability to characterize multiple samples in a single experiment, opening the door to a highly sensitive multi-analyte detection technology.
000165382 536__ $$9info:eu-repo/grantAgreement/ES/AEI/AEI PID2022-137779OB-C41$$9info:eu-repo/grantAgreement/ES/AEI/AEI PID2022-140923NB-C21$$9info:eu-repo/grantAgreement/ES/DGA/E09-23R$$9info:eu-repo/grantAgreement/ES/DGA/E31-23R$$9info:eu-repo/grantAgreement/ES/MICINN/CEX2020-001039-S$$9info:eu-repo/grantAgreement/EUR/MICINN/TED2021-131447B-C21$$9info:eu-repo/grantAgreement/EUR/MICINN/TED2021-131447B-C22$$9info:eu-repo/grantAgreement/ES/MICIU/CEX2023-001286-S$$9info:eu-repo/grantAgreement/ES/MINECO/PID2020-118329RB-I00
000165382 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc$$uhttps://creativecommons.org/licenses/by-nc/4.0/deed.es
000165382 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000165382 700__ $$aRodriguez, David
000165382 700__ $$aPallarés, María Carmen
000165382 700__ $$aGranados, Daniel
000165382 700__ $$aRoubeau, Olivier
000165382 700__ $$aLuis, Fernando
000165382 700__ $$aGomez, Alicia
000165382 700__ $$0(orcid)0000-0001-7460-5916$$aLostao, Anabel
000165382 773__ $$g(2025), [9 pp.]$$pNanoscale$$tNanoscale$$x2040-3364
000165382 8564_ $$s6488533$$uhttps://zaguan.unizar.es/record/165382/files/texto_completo.pdf$$yVersión publicada
000165382 8564_ $$s2715177$$uhttps://zaguan.unizar.es/record/165382/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000165382 909CO $$ooai:zaguan.unizar.es:165382$$particulos$$pdriver
000165382 951__ $$a2026-01-07-18:53:33
000165382 980__ $$aARTICLE