F
Fausto Sanz
Researcher at University of Barcelona
Publications - 191
Citations - 5714
Fausto Sanz is an academic researcher from University of Barcelona. The author has contributed to research in topics: Force spectroscopy & Lipid bilayer. The author has an hindex of 39, co-authored 191 publications receiving 5272 citations. Previous affiliations of Fausto Sanz include Spanish National Research Council & University of Salamanca.
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Effect of ion-binding and chemical phospholipid structure on the nanomechanics of lipid bilayers studied by force spectroscopy.
TL;DR: It is experimentally proved that the amount of ions present in the measuring system has a strong effect on the force needed to puncture a 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayer with an atomic force microscope tip, highlighting the role that monovalent cations play upon membrane stability.
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Effect of Temperature on the Nanomechanics of Lipid Bilayers Studied by Force Spectroscopy
TL;DR: It is experimentally proved that the force needed to puncture the lipid bilayer (Fy) is temperature dependent, and a "well" in the Fy versus temperature plot occurs around TM, thus proving an "anomalous mechanical softening" around TM.
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Nanomechanics of lipid bilayers by force spectroscopy with AFM: A perspective
Sergi Garcia-Manyes,Fausto Sanz +1 more
TL;DR: The goal of this review is to illustrate how novel experiments have provided a new vista on membrane mechanics in a confined area within the nanometer realm, where most of the specific molecular interactions take place.
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Influence of cholesterol on the phase transition of lipid bilayers: a temperature-controlled force spectroscopy study.
TL;DR: It is proved that low Chol contents lead to a phase-segregated system, whereas high contents of Chol can give a homogeneous bilayer, and the AFM-FS technique is validated as an ideal platform to differentiate phase coexistence and transitions in lipid bilayers.
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Fine structure study of Aβ1-42 fibrillogenesis with atomic force microscopy
Muriel Arimon,Ismael Díez-Pérez,Marcelo J. Kogan,Nuria Durany,Ernest Giralt,Fausto Sanz,Xavier Fernàndez-Busquets +6 more
TL;DR: The results presented provide nanometric resolution of the main structures characteristic of the several steps from monomeric Aβ1–42 to mature fibrils in vitro, and are consistent with the existence of a ∼100‐nm long basic protofibril unit that is a key fibril building block.