Discovering the molecular recognition of technological solids by mutant self-assembling peptides

What is it about?

Frequency modulated atomic force microscopy was utilized to reveal the molecular architecture of genetically designed and point mutated peptides and their self-organizations. Each formed single-molecule thick, distinct biological crystals on atomically flat graphite and MoS2 surfaces, offering a potential platform for hybrid technologies such as bioelectronics, biosensors, and protein arrays.

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Why is it important?

Neither the molecular recognition of solid-state objects by a ‘living’ molecule has been so clearly observed before, nor have its details been described as chiral, both adding to the significance of the results presented in this publication. On the one hand, from the biology perspective, there is now ample data and details on how mutations lead to molecular conformational changes and the resultant function of the peptides, which can be expanded into the behavior of proteins, with significance in genetic mutations and effective drug design. And on the other hand, coherent hybridization suggests that animate and inanimate nanoscale objects are stably present at the same soft interface, forming an exclusive molecular bridge that could be best described by seamlessly integrating biology with solid-state devices. If so, based on this study, scientists and technologists are expected to enormously widen the repertoire of the molecular basis of future bio/nano devices by using the simple molecular biology tool of mutation.