Molecular sensitised probe for amino acid recognition within peptide sequences

0581766 - FZÚ 2024 RIV US eng J - Journal Article
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
R&D Projects: GA ČR(CZ) GX20-13692X
Research Infrastructure: e-INFRA CZ II - 90254; CzechNanoLab II - 90251
Institutional support: RVO:68378271
Keywords : SPM * recogniton * peptides * DFT
OECD category: Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)
Impact factor: 16.6, year: 2022
Method of publishing: 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.
Permanent Link: https://hdl.handle.net/11104/0349912