Possible bi-stable structures of pyrene-butanoic-acid-linked protein molecules adsorbed on graphene: Theoretical study

Submitting author affiliation:
Graduate School of Science, University of Hyogo, Kouto, Kamigori-cho, Ako-gun, Hyogo, Japan

Beilstein Arch. 2023, 202359. https://doi.org/10.3762/bxiv.2023.59.v1

Published 11 Dec 2023

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This preprint has not been peer-reviewed. When a peer-reviewed version is available, this information will be updated.


We theoretically analyze possible multiple conformations of protein molecules immobilized by 1-pyrenebutanoic-acid-succinimidyl-ester (PASE) linkers on graphene. The activation barrier between two bi-stable conformations exhibited by PASE is confirmed to be based on the steric hindrance effect between a hydrogen on the pyrene group and a hydrogen on the alkyl group of this molecule. Even after the protein is supplemented, this steric hindrance effect remains if the local structure of the linker consisting of an alkyl group and a pyrene group is maintained. Therefore, it is likely that the kinetic behavior of a protein immobilized with a single PASE linker exhibits an activation barrier-type energy surface between the bi-stable conformations on graphene. We discuss the expected protein sensors when this type of energy surface appears and provide a guideline for improving the sensitivity, especially as an oscillator-type biosensor.

Keywords: PASE; protein; surface adsorption; biosensor; DFT

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When a peer-reviewed version of this preprint is available, this information will be updated in the information box above. If no peer-reviewed version is available, please cite this preprint using the following information:

Oishi, Y.; Kitatani, M.; Kusakabe, K. Beilstein Arch. 2023, 202359. doi:10.3762/bxiv.2023.59.v1

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