title: Molecular tweezers target a protein-protein interface and thereby modulate complex formation.
abstract: Molecular tweezers for lysine and arginine select a few residues on a protein surface and by their unique complexation mode disrupt a critical protein-protein interaction. Detailed structural information was gained by NMR experiments, strongly supported by QM/MM calculations and further substantiated by ITC, fluorescence anisotropy, ELISA and bio-layer-interference studies.
authors.affiliation: University of Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany. peter.bayer@uni-due.de.
authors.forename: F
authors.identifier: http://orcid.org/0000-0003-0608-202X
authors.initials: F
authors.lastname: Trusch
authors.affiliation: University of Duisburg-Essen, Research Group Organic Chemistry, 45117 Essen, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Kowski
authors.affiliation: Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Bravo-Rodriguez
authors.affiliation: University of Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany. peter.bayer@uni-due.de.
authors.forename: C
authors.initials: C
authors.lastname: Beuck
authors.affiliation: University of Duisburg-Essen, Research Group Organic Chemistry, 45117 Essen, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Sowislok
authors.affiliation: University of Duisburg-Essen, Research Group Organic Chemistry, 45117 Essen, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Wettig
authors.affiliation: University of Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany. peter.bayer@uni-due.de.
authors.forename: A
authors.initials: A
authors.lastname: Matena
authors.affiliation: Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.
authors.forename: E
authors.initials: E
authors.lastname: Sanchez-Garcia
authors.affiliation: University of Duisburg-Essen, Research Group Molecular Biology I, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Meyer
authors.affiliation: University of Duisburg-Essen, Research Group Organic Chemistry, 45117 Essen, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Schrader
authors.affiliation: University of Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany. peter.bayer@uni-due.de.
authors.forename: P
authors.identifier: http://orcid.org/0000-0003-0435-7202
authors.initials: P
authors.lastname: Bayer
mesh_terms: D001120:Arginine / Q000737:chemistry; D004797:Enzyme-Linked Immunosorbent Assay; D005454:Fluorescence Polarization; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D013499:Surface Properties
chemical_list: D011506:Proteins; D001120:Arginine; D008239:Lysine