Suchergebnisse

This study was supported by projects CTQ2017-86568-R and FIS2017-85954-R (Ministerio de Economia, Industria y Competitividad, MINECO, and Agencia Estatal de Investigacion, AEI, Spain, cofunded by Fondo Europeo de Desarrollo Regional, FEDER, European Union), and by FEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades (Spain) project P18-FR-3533. We want to thank "Unidad de Excelencia Quimica aplicada a Biomedicina y Medioambiente" of the University of Granada. Thanks go to the CIC personnel of the University of Granada for technical assistance. We thank the Centro de Servicios de Informatica y Redes de Comunicaciones (CSIRC), Universidad de Granada, for providing the computing time. Authors acknowledge to Dr Rosario Herranz and Dr Francisco Fueyo-Gonzalez for the fluorophore 9-azetidinyl-5-butyl-quinolimide (AQui) used in this study, which was synthesized at Instituto de Quimica Medica-CSIC (IQM-CSIC) with the support of the Ministerio de Ciencia e Innovacion/Agencia Estatal de Investigacion grant FU2015-67284-R. ; Making use of the combination of multiparametric Fluorescence Lifetime Imaging Microscopy (FLIM) and single-molecule Fluorescence Lifetime Correlation Spectroscopy (FLCS), we have been able to study for the early stages of the fluorenylmethyloxycarbonyl-diphenylalanine (Fmoc-FF) self-assembly process with single-molecule resolution, the kinetics of fiber formation, the packaging of the peptides within the fibers and the capacity of the peptides to reassemble after disruption (self-healing) in the presence of different metallic cations. Other techniques such as FTIR, TEM, DSC and DFT calculations support our findings. The impact that the mechanism of self-assembly has on the physical (rigidity and self-healing) properties of the resulting gels have also been evaluated by rheology. Calcium ions are able to promote the self-assembly of Fmoc-FF faster and more efficiently, forming more rigid hydrogels than do cesium ions. The reasons behind this effect may be explained by the different capacities that these two cations have to coordinate with the peptide, modulate its hydrophobicity and stabilize the water-solute interphase. These findings shed light on the impact that small changes have on the process of self-assembly and can help to understand the influence of the environmental conditions on the in vivo uncontrolled self-assembly of certain proteins. ; Ministerio de Economia, Industria y Competitividad, MINECO CTQ2017-86568-R FIS2017-85954-R ; Agencia Estatal de Investigacion, AEI, Spain CTQ2017-86568-R FIS2017-85954-R ; Fondo Europeo de Desarrollo Regional, FEDER, European Union CTQ2017-86568-R FIS2017-85954-R ; FEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades (Spain) P18-FR-3533 ; Ministerio de Ciencia e Innovacion/Agencia Estatal de Investigacion FU2015-67284-R