RT Journal Article
T1 Using Surface Enhanced Raman Scattering to Analyze the Interactions of Protein Receptors with Bacterial Quorum Sensing Modulators
A1 Costas, Celina
A1 López Puente, Vanesa
A1 Bodelón, Gustavo
A1 González Bello, Concepción
A1 Pérez Juste, Jorge
A1 Pastoriza Santos, Isabel
A1 Liz-Marzán, Luis M.
K1 Nanoplasmonics
K1 SERS
K1 Quorum sensing
K1 Protein receptors
K1 Pseudomonas aeruginosa
AB Many members of the LuxR family of quorum sensing (QS) transcriptional activators, including LasR of Pseudomonas aeruginosa, are believed to require appropriate acyl-homoserine lactone (acyl-HSL) ligands to fold into an active conformation. The failure to purify ligand-free LuxR homologues in nonaggregated form at the high concentrations required for their structural characterization has limited the understanding of the mechanisms by which QS receptors are activated. Surface-enhanced Raman scattering (SERS) is a vibrational spectroscopy technique that can be applied to study proteins at extremely low concentrations in their active state. The high sensitivity of SERS has allowed us to detect molecular interactions between the ligand-binding domain of LasR (LasRLBD) as a soluble apoprotein and modulators of P. aeruginosa QS. We found that QS activators and inhibitors produce differential SERS fingerprints in LasRLBD, and in combination with molecular docking analysis provide insight into the relevant interaction mechanism. This study reveals signal-specific structural changes in LasR upon ligand binding, thereby confirming the applicability of SERS to analyze ligand-induced conformational changes in proteins
PB American Chemical Society
SN 1936-0851
YR 2015
FD 2015-04-30
LK http://hdl.handle.net/10347/16921
UL http://hdl.handle.net/10347/16921
LA eng
NO Costas, C., López-Puente, V., Bodelón, G., González-Bello, C., Pérez-Juste, J., Pastoriza-Santos, I., & Liz-Marzán, L. (2015). Using Surface Enhanced Raman Scattering to Analyze the Interactions of Protein Receptors with Bacterial Quorum Sensing Modulators. ACS Nano, 9(5), 5567-5576. doi: 10.1021/acsnano.5b01800
DS Minerva
RD 24 abr 2026