Our group has a long-standing tradition in studying DNA-protein interactions with the AFM. In two recent collaborations we investigated how a small peptide binds and condense dsDNA using force spectroscopy methods and how Rep proteins bind to a specific region in the replication origin of plasmids.
Interactions between self-aggregating peptides and nucleic acids are underlying processes in several human diseases such us Alzheimer and Parquison. We studied an hydrophobic anticancer peptide and characterised the dynamics and mechanics of its interaction with ssDNA and dsDNA. On the other hand, we found that Rep proteins bind simultaneously to the specific dsDNA iterons region and to one of the AT-rich strands facilitating the opening of the replication bubble.
Univ. Barcelona: F. Ritort´s Group
Univ. Gdansk: I. Konieczny´s Group
Univ. of Pittsburg: S. Khan and S. Leuba Groups
UCM. Biochemistry Dept.: J. Perez-Gil´s Group
CSIC. CIB: M. Oliva´s Group
J. Camunas-Soler et al. ACSnano 7 (6), 5102-5114 (2013).
Electrostatic binding and hydrophobic collapse of peptide-nucleic acid aggregates quantified using force spectroscopy”
Wegrzyn et al. Nucleic Acids Res. In press 16 MAY (2014).
Sequence-specific interactions of Rep proteins with ssDNA in the AT-rich region of the plasmid replication origin
Pastrana* Carrasco* et al. Nucleic Acids Research 44(18), 8885-8896 Published Online Aug3 (2016).
Force and twist dependence of RepC nicking activity on torsionally-constrained DNA molecules