Biophysical interactions unit

The unit provides a service to scientist from the IQM, other CSIC institutes or external centers as public research organisms, universities or private companies. Our unit is equipped with a surface plasmon resonance technology (SPR) which allows to detect interactions in real time between two or more biomolecules without any kind of label. The specificity of the interactions and kinetic and affinity parameters are the main information which can be obtain with a SPR experiment. The data analysis provides the rate constants and the affinity constant of the complex (KD, kon and koff).

Besides, it can be useful for determining thermodynamic parameters through the measurement at different temperatures.

The high sensibility of this technique is the main advantage, fundamental in the drug- receptor interactions. The different samples that can be analyzed are biomolecules (proteins, peptides, lipids..), drugs, or organic and inorganic compounds.

On the other hand, the unit also has an isothermal titration calorimeter (ITC) equipment. ITC contains a detection system which is allowed to work with any kind of biomolecule and it is based in the absorption or release of heat after the interaction between two molecules. With this technology we can obtain information about the affinity (Kd), enthalpy, entropy and stoiquiometry of the reaction in one single experiment. One of the main advantages is the little amount of volume which it can work: about 200. With ITC technology we can measure interactions of proteins, polysaccharides, lipids, small molecules (drugs) etc. Besides, the equipment can work with different kind of buffers, DMSO, etc. Finally, the sensitivity of this technology is very high, which is very important for detecting low and high affinity interactions.

Both technologies, SPR and ITC, can be used for detecting this kind of systems:

    • Drug-receptor interaction
    • Protein-protein interaction
    • Protein-carbohydrate interaction
    • Protein-lipid interaction
    • Enzyme-substrate interaction
    • Antigen-antibody interaction
    • Drug design (characterization of modified compounds)
    • DNA-protein and DNA-small molecule interaction

Finally, the unit recently has acquired a new technology based in the intrinsic fluorescence with an increase of temperature (Nano DSF). This equipment provides the information about the quality of the sample and the denaturalization profile of the proteins. With Nano DSF the functionality of the proteins can be determined in the absence and in the presence of ligands. Besides, we can detect some contaminants of the samples, establish a comparison between two batch of protein or discriminate between the buffers destined to protein storage.

PUBLICATIONS

Butrón D, Zamora-Carreras H, Devesa I, Treviño MA, Abian O, Velázquez-Campoy A, Bonache MÁ, Lagartera L, Martín-Martínez M, González-Rodríguez S, Baamonde A, Fernández-Carvajal A, Ferrer-Montiel A, Jiménez MÁ, González-Muñiz R. DD04107-Derived neuronal exocytosis inhibitor peptides: Evidences for synaptotagmin-1 as a putative target.  Bioorg Chem (2021) 115:105231. doi: 10.1016/j.bioorg.2021.105231.

 

Sainz-Ramos M, Villate-Beitia I, Gallego I, Al Qtaish N, Menéndez M, Lagartera L, Grijalvo S, Eritja R, Puras G, Pedraz JL. Correlation between Biophysical Properties of Niosomes Elaborated with Chloroquine and Different Tensioactives and Their Transfection Efficiency. Pharmaceutics. (2021) 13:1787. doi: 10.3390/pharmaceutics13111787.

 

Benavente JL, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella MA, Sánchez-Barrena MJ, Albert A. Life Sci Alliance. The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Sci Alliance. (2021) 4(10) doi: 10.26508/lsa.202101152

 

Vessella G, Vázquez JA, Valcárcel J, Lagartera L, Monterrey DT, Bastida A, García-Junceda E, Bedini E, Fernández-Mayoralas A, Revuelta J. Deciphering Structural Determinants in Chondroitin Sulfate Binding to FGF-2: Paving the Way to Enhanced Predictability of their Biological Functions.  Polymers. (2021) 3:313. doi: 10.3390/polym13020313.

 

Cercos P, Peraza DA, Miaja P, Merinero YG, Lagartera L, Martín-MartínezM, Naranjo JR, Gutiérrez-Rodríguez M, Valenzuela C. Identification of IQM-266 as a New Activator of KV4 Currents Mediated by the Accessory Protein DREAM. Front Mol Neurosci (2019) 12:1-14

 

Lopez-Hurtado A, Peraza DA, Cercos P, Lagartera L, Gonzalez P, Dopazo XM, Herranz R, Gonzalez T, Martin-Martinez M, Mellström B, Naranjo JR, Valenzuela C, Gutierrez-Rodriguez Targeting the neuronal calcium sensor DREAM with small-molecules for Huntington’s disease treatment.M. Sci Rep (2019) 9:7260.

FARES AND CONTACT

Equipos: BIACORE X-100, MicroCal PEAQ-ITC y Tycho NT6

The development of an experiment and the maintenance of each equipment have an intrinsic price. For this reason, the price is related to cover the optimal operation of the equipment. These prices offer next support:

    • Experimental design.
    • Experimental acquisition dates.
    • Buffers preparation.
    • Supply of experimental data.
    • Report about the interaction with the parameters associated as Kds, DH, DS, etc.

 

For any kind of information please contact us:

Dra. Laura Lagartera Ortiz

Instituto Química Médica

915622900 Ext 356

l.lagartera@iqm.csic.es

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