000117628 001__ 117628
000117628 005__ 20240319081008.0
000117628 0247_ $$2doi$$a10.3390/biom12040594
000117628 0248_ $$2sideral$$a129190
000117628 037__ $$aART-2022-129190
000117628 041__ $$aeng
000117628 100__ $$0(orcid)0000-0003-3459-8605$$aMarcuello, C.
000117628 245__ $$aMolecular recognition of proteins through quantitative force maps at single molecule level
000117628 260__ $$c2022
000117628 5060_ $$aAccess copy available to the general public$$fUnrestricted
000117628 5203_ $$aIntermittent jumping force is an operational atomic-force microscopy mode that produces simultaneous topography and tip-sample maximum-adhesion images based on force spectroscopy. In this work, the operation conditions have been implemented scanning in a repulsive regime and applying very low forces, thus avoiding unspecific tip-sample forces. Remarkably, adhesion images give only specific rupture events, becoming qualitative and quantitative molecular recognition maps obtained at reasonably fast rates, which is a great advantage compared to the force–volume modes. This procedure has been used to go further in discriminating between two similar protein molecules, avidin and streptavidin, in hybrid samples. The adhesion maps generated scanning with biotiny-lated probes showed features identified as avidin molecules, in the range of 40–80 pN; meanwhile, streptavidin molecules rendered 120–170 pN at the selected working conditions. The gathered results evidence that repulsive jumping force mode applying very small forces allows the identification of biomolecules through the specific rupture forces of the complexes and could serve to identify receptors on membranes or samples or be applied to design ultrasensitive detection technologies.
000117628 536__ $$9info:eu-repo/grantAgreement/ES/CSIC/QTP-2103003$$9info:eu-repo/grantAgreement/ES/DGA-FEDER/E35-20R$$9info:eu-repo/grantAgreement/ES/DGA/LMP58-18$$9info:eu-repo/grantAgreement/ES/MICINN-AEI/PID2019-103901GB-I00
000117628 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000117628 590__ $$a5.5$$b2022
000117628 592__ $$a1.074$$b2022
000117628 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b70 / 285 = 0.246$$c2022$$dQ1$$eT1
000117628 593__ $$aBiochemistry$$c2022$$dQ1
000117628 593__ $$aMolecular Biology$$c2022$$dQ2
000117628 594__ $$a8.3$$b2022
000117628 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000117628 700__ $$aMiguel, R. de
000117628 700__ $$0(orcid)0000-0001-7460-5916$$aLostao, A.
000117628 773__ $$g12, 4 (2022), 594 [15 pp.]$$tBiomolecules$$x2218-273X
000117628 8564_ $$s3128931$$uhttps://zaguan.unizar.es/record/117628/files/texto_completo.pdf$$yVersión publicada
000117628 8564_ $$s2750213$$uhttps://zaguan.unizar.es/record/117628/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000117628 909CO $$ooai:zaguan.unizar.es:117628$$particulos$$pdriver
000117628 951__ $$a2024-03-18-14:48:44
000117628 980__ $$aARTICLE