Molecular sensitised probe for amino acid recognition within peptide sequences

0581766 - FZÚ 2024 RIV US eng J - Článek v odborném periodiku
WU, X. - Borca, B. - Sen, S. - Koslowski, S. - Abb, S. - Rosenblatt, D.P. - Gallardo Caparrós, Aurelio Jesús - Mendieta Moreno, Jesús Ignacio - Nachtigall, Matyáš - Jelínek, Pavel - Rauschenbach, S. - Kern, K. - Schlickum, U.
Molecular sensitised probe for amino acid recognition within peptide sequences.
Nature Communications. Roč. 14, č. 1 (2023), č. článku 8335. E-ISSN 2041-1723
Grant CEP: GA ČR(CZ) GX20-13692X
Výzkumná infrastruktura: e-INFRA CZ II - 90254; CzechNanoLab II - 90251
Institucionální podpora: RVO:68378271
Klíčová slova: SPM * recogniton * peptides * DFT
Obor OECD: Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)
Impakt faktor: 16.6, rok: 2022
Způsob publikování: Open access

The combination of low-temperature scanning tunnelling microscopy with a mass-selective electro-spray ion-beam deposition established the investigation of large biomolecules at nanometer and sub-nanometer scale. A selective intermolecular interaction between the sensitiser attached at the tip-apex and the target amino acid on the surface induces an enhanced tunnelling conductance of one specific spectral feature, which can be mapped in spectroscopic imaging. Density functional theory calculations suggest a mechanism that relies on conformational changes of the sensitiser that are accompanied by local charge redistributions in the tunnelling junction, which, in turn, lower the tunnelling barrier at that specific part of the peptide.
Trvalý link: https://hdl.handle.net/11104/0349912