Reverse engineering of an affinity-switchable molecular interaction characterized by atomic force microscopy single-molecule force spectroscopy.
Tunable and switchable interaction between molecules is a key for regulation and control of cellular processes. The translation of the underlying physicochemical principles to synthetic and switchable functional entities and molecules that can mimic the corresponding molecular functions is called reverse molecular engineering. We quantitatively investigated autoinducer-regulated DNA-protein interaction in bacterial gene regulation processes with single atomic force microscopy (AFM) molecule force spectroscopy in vitro, and developed an artificial bistable molecular host-guest system that can be controlled and regulated by external signals (UV light exposure and thermal energy). The intermolecular binding functionality (affinity) and its reproducible and reversible switching has been proven by AFM force spectroscopy at the single-molecule level. This affinity-tunable optomechanical switch will allow novel applications with respect to molecular manipulation, nanoscale rewritable molecular memories, and/or artificial ion channels, which will serve for the controlled transport and release of ions and neutral compounds in the future.
Experimental Biophysics & Applied Nanoscience, Department of Physics, Bielefeld University, Bielefeld, Germany. dario.anselmetti@physik.uni-bielefeld.de
Dario
D
Anselmetti
Frank Wilco
FW
Bartels
Anke
A
Becker
Björn
B
Decker
Rainer
R
Eckel
Matthew
M
McIntosh
Jochen
J
Mattay
Patrik
P
Plattner
Robert
R
Ros
Christian
C
Schäfer
Norbert
N
Sewald
D001426:Bacterial Proteins / Q000737:chemistry* / Q000528:radiation effects; D047250:Calixarenes / Q000737:chemistry / Q000528:radiation effects; D004247:DNA / Q000737:chemistry* / Q000528:radiation effects; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods*; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000528:radiation effects; D010777:Photochemistry; D015202:Protein Engineering; D016962:Sinorhizobium meliloti / Q000737:chemistry; D013057:Spectrum Analysis / Q000295:instrumentation / Q000379:methods; D013314:Stress, Mechanical; D013696:Temperature; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; C466160:resorcinarene; D047250:Calixarenes; D010649:Phenylalanine; D004247:DNA