Begoña Sot Sanz

 

Unit: Complex Disorders

E-mail: MBegona.Sot@ciemat.es

Phone: +34914962674

Dr. Begoña Sot early years’ scientific trajectory was focused on the study of the molecular mechanism of protein´s activity.  She learned all the necessary techniques to understand proteins: molecular biology, biochemistry, biophysics, and structural biology. During the doctoral and postdoctoral stays in Spanish and European centers (UPV-EHU, MRC, Max-Plank Institute, CNB), she studied different disease related proteins, like kRas, P53 or alpha-Synuclein. This extensive knowledge about proteins showed her the potential of their use in biotechnology and biomedicine. She then joined IMDEA Nanociencia research center to lead the Protein Engineering Laboratory with the objective to implement proteins as nanotechnology and nanomedical tools. Since 2017 her research is focused on the design of non-viral vehicles for the efficient and specific delivery of engineered CRISPR proteins. The IMDEA-nanociencia multidisciplinary environment allowed her collaboration with experts in nanoparticles and their use as delivery vehicles. Finally, in 2021 she joined the “Unity of innovative medicine” in CIEMAT, where she applies her knowledge in nanomedicine for the design of treatments for different diseases. She is author of 28 peer-reviewed articles (H-index 15), 7 of them as corresponding author.

 

Publications:

  1. CASCADE: Naked eye-detection of SARS-CoV-2 using Cas13a and gold nanoparticles. López-Valls M, et al., Anal Chim Acta. 2022;1205:339749. doi: 10.1016/j.aca.2022.339749.
  1. CRISPR/Cas technology as a promising weapon to combat viral infections.Escalona-Noguero C, López-Valls M, Sot B. Bioessays. 2021;43(4):e2000315. doi: 10.1002/bies.202000315.
  1. Combining Ag and γ-Fe2O3 properties to produce effective antibacterial nanocomposites. Luengo Y, et al.,  Colloids Surf B Biointerfaces. 2020; 194:111178. doi: 10.1016/j.colsurfb.2020.111178.
  1. Role of α-Synuclein Regions in Nucleation and Elongation of Amyloid Fiber Assembly. Gallardo J et al., ACS Chem Neurosci. 2020; 11(6):872-879. doi: 10.1021/acschemneuro.9b00527.
  1. Domain topology of human Rasal. Cuellar J, et al., Biol Chem. 2017; 399(1):63-72. doi: 10.1515/hsz-2017-0159.
  1. The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction. Sot B, et al., Sci Rep. 2017; 7:40859. doi: 10.1038/srep40859.
  1. Molecular chaperones: functional mechanisms and nanotechnological applications. Fernández-Fernández MR, et al.,  Nanotechnology. 2016; 27(32):324004. doi: 10.1088/0957-4484/27/32/324004.
  1. Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes. Sot B, et al.,  Proc Natl Acad Sci U S A. 2013; 110(1):111-6. doi: 10.1073/pnas.1201658110.
  1. Unravelling the mechanism of dual-specificity GAPs. Sot B et al., EMBO J. 2010; 29(7):1205-14. doi: 10.1038/emboj.2010.20.
  1.  Comparative biophysical characterization of p53 with the pro-apoptotic BAK and the anti-apoptotic BCL-xL. Sot B, et al., J Biol Chem. 2007; 282(40):29193-200. doi: 10.1074/jbc.M705544200.
  1. Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study. Sot B, et al., Protein Sci. 2005; 14(9):2267-74. doi: 10.1110/ps.051469605.
  1. GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites. Sot B, et al., J Biol Chem. 2003; 278(34):32083-90. doi: 10.1074/jbc.M303958200.
  1. Salt bridges at the inter-ring interface regulate the thermostat of GroEL. Sot B, et al.,  J Biol Chem. 2002 Sep 13;277(37):34024-9. doi: 10.1074/jbc.M205733200.