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web del Instituto de Biología Molecular y Celular

Group name: PROTEIN BIOTECHNOLOGY


We develop basic research on the structure and folding of proteins by the acquisition of structural and thermodynamic data. Many of our results are oriented towards technological transfer, more precisely those dealing with the design of new antibiotics and the setup of novel systems of purification and immobilization of recombinant proteins. Our studies are centered basically in three lines:

1. Design, selection and evaluation of new antimicrobials against Streptococcus pneumoniae (pneumococcus) based on small molecules or in multivalent nanoparticles.

2. The C-LytA affinity tag, that serves as a model to study the folding and engineering of repeat proteins and constitutes an efficient affinity tag for the single-step chromatographic purification and immobilization of recombinant proteins from nano- to macrosurfaces, including enzymatic electrodes.

3.- Bioplastics. Natural, biodegradable plastics of bacterial origin that may constitute an alternative to the use of petroleum derivatives. We study the structure and function of several proteins involved in the synthesis, stability and degradation of these bioplastics, and the immobilization of proteins on these polymers.

Laboratory expertise includes:

- Thermodynamic analysis of protein stability.

- Spectroscopy (absorption, fluorescence, circular dichroism).

- Protein engineering.

- Nanobiotechnology.

RESEARCH HIGHLIGHTS

Angew Chem Int Ed Engl. 2015 Nov 9;54(46):13673-7. doi: 10.1002/anie.201505700. Epub 2015 Sep 17. Aromatic Esters of Bicyclic Amines as Antimicrobials against Streptococcus pneumoniae. Retamosa M, Díez-Martínez R, Maestro B, García-Fernández E, de Waal B, Meijer EW, García P, Sanz JM.

Our investigations on the choline-binding proteins (CBPs) from the Streptococcus pneumoniae pathogen (pneumococcus), a major cause of diseases such as meningitis an pneumoniae, allowed the identification of molecules able to inhibit the binding of such polypeptides to the bacterial surface. The efficiency of these molecules was increased by several orders of magnitude upon multivalent disposition on dendrimeric nanoparticles. All these molecules cause bacterial death and lysis, so they may be considered as a new line of antimicrobials against pneumococcus that might help solve the current problems of antibiotic resistance displayed by this microorganism.

PLoS One. 2014 Jan 31;9(1):e87995. doi: 10.1371/journal.pone.0087995. eCollection 2014. Specific and reversible immobilization of proteins tagged to the affinity polypeptide C-LytA on functionalized graphite electrodes. Bello-Gil D, Maestro B, Fonseca J, Feliu JM, Climent V, Sanz JM.

Takin advantage of the affinity of pneumococcal CBPs for choline and structural analogs, we have developed an immobilization system of enzymes on electrodes. With this procedure, a graphite electrode is functionalized with diethylaminoethyl groups, and acts as a support for the fast, strong and reversible immobilization of enzymes fused to the choline-binding module CD-LytA. The reaction products can be detected electrochemically. This method allows the creation of tailored biosensors simply building the corresponding fusion with C-LytA.

STAFF

Jesús Miguel Sanz Morales

Manuel Sánchez Angulo (Visiting scientist)

POSTDOCTORAL SCIENTISTS

Beatriz Maestro García-Donas

Ph. D. STUDENTS

Emma Roig Molina

TECHNICIANS

Maite Garzón Cabrerizo

PUBLICATIONS (ARTICLES)

  1. Angew Chem Int Ed Engl. 2015 Nov 9;54(46):13673-7. doi: 10.1002/anie.201505700. Epub 2015 Sep 17. Aromatic Esters of Bicyclic Amines as Antimicrobials against Streptococcus pneumoniae. de Gracia Retamosa M, Díez-Martínez R, Maestro B, García-Fernández E, de Waal B, Meijer EW, García P, Sanz JM.
  2. Chemistry. 2015 May 26;21(22):8076-89. doi: 10.1002/chem.201500447. Epub 2015 Apr 27.
  3. Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA. Zamora-Carreras H, Maestro B, Strandberg E, Ulrich AS, Sanz JM, Jiménez M.
  4. PLoS One. 2014 Jan 31;9(1):e87995. doi: 10.1371/journal.pone.0087995. eCollection 2014. Specific and reversible immobilization of proteins tagged to the affinity polypeptide C-LytA on functionalized graphite electrodes. Bello-Gil D, Maestro B, Fonseca J, Feliu JM, Climent V, Sanz JM.
  5. PLoS One. 2013;8(2):e56904. doi: 10.1371/journal.pone.0056904. Epub 2013 Feb 15. A new family of intrinsically disordered proteins: structural characterization of the major phasin PhaF from Pseudomonas putida KT2440. Maestro B, Galán B, Alfonso C, Rivas G, Prieto MA, Sanz JM.
  6. Chem Commun (Camb). 2011 Jun 7;47(21):5997-9. doi: 10.1039/c0cc05605g. Epub 2011 Apr 21. Choline dendrimers as generic scaffolds for the non-covalent synthesis of multivalent protein assemblies. Hernández-Rocamora VM, Reulen SW, de Waal B, Meijer EW, Sanz JM, Merkx M.
  7. Protein Eng Des Sel. 2011 Jan;24(1-2):113-22. doi: 10.1093/protein/gzq087. Epub 2010 Nov 4. Structural autonomy of a β-hairpin peptide derived from the pneumococcal choline-binding protein LytA. Maestro B, Santiveri CM, Jiménez MA, Sanz JM.
  8. Angew Chem Int Ed Engl. 2009;48(5):948-51. doi: 10.1002/anie.200803664. Multivalent choline dendrimers as potent inhibitors of pneumococcal cell-wall hydrolysis. Hernández-Rocamora VM1, Maestro B, de Waal B, Morales M, García P, Meijer EW, Merkx M, Sanz JM.

PATENTS

Retamosa, M.G.; Maestro, B.; Díez, R.; García, P.; Sanz, J.M.ES2526580. Uso de un compuesto de fórmula (I) como bactericida frente a Streptococcus. España. 23/10/2015. Universidad Miguel Hernández de Elche y CSIC.

Maestro B; Arévalo M; Hernández VM; Cebolla A; Sanz JM. ES2321788. Dominios de afinidad a colina para mejorar la expresión, inmovilización y purificación de polipéptidos. España. 11/03/2010. Universidad Miguel Hernández. Biomedal S.L. (Sevilla).

Sanz JM; Maestro B; Arévalo M; Velasco I; Cebolla A. ES2319844. Procedimientos de separación de proteínas recombinantes en sistemas acuosos de dos fases. España. 01/02/2010. Universidad Miguel Hernández y Biomedal S.L.. Biomedal S.L. (Sevilla). International extensions: USA (US8329877), Europe (EP2196470), Japan (JP5271354).