Hydraulic Activation of the AsLOV2 photoreceptor

TY - UNPB

T1 - Hydraulic Activation of the AsLOV2 photoreceptor

AU - Maity, Shiny

AU - Sheppard, Jackson

AU - Russell, Hannah

AU - Han, Chungta

AU - Epstein, Leah

AU - Johnson, Bruce A.

AU - Price, Brad

AU - Han, Ruixian

AU - Potnuru, Lokeswara Rao

AU - Cui, Jinlei

AU - Sherwin, Mark S.

AU - Shea, Joan-Emma

AU - Lovett, Janet E.

AU - Gardner, Kevin H.

AU - Han, Songi

PY - 2025/6/25

Y1 - 2025/6/25

N2 - How proteins transduce environmental signals into mechanical motion remains a central question in biology. This study tests the hypothesis that blue light activation of AsLOV2 gives rise to concerted water movement that induce protein conformational extensions. Using electron and nuclear magnetic resonance spectroscopy, along with atomistic molecular dynamics simulations at high pressure, we find that activation, whether initiated by blue light or high pressure, is accompanied by selective expulsion of low-entropy, tetrahedrally coordinated “wrap” water from hydrophobic regions of the protein. These findings suggest that interfacial water serves as functional constituents to help reshape the protein’s free energy landscape during activation. Our study highlights hydration water as an active medium with the capacity to drive long-range conformational changes underlying protein mechanics and offers a new conceptual understanding for engineering externally controllable protein actuators for biomedical studies to smart materials.

AB - How proteins transduce environmental signals into mechanical motion remains a central question in biology. This study tests the hypothesis that blue light activation of AsLOV2 gives rise to concerted water movement that induce protein conformational extensions. Using electron and nuclear magnetic resonance spectroscopy, along with atomistic molecular dynamics simulations at high pressure, we find that activation, whether initiated by blue light or high pressure, is accompanied by selective expulsion of low-entropy, tetrahedrally coordinated “wrap” water from hydrophobic regions of the protein. These findings suggest that interfacial water serves as functional constituents to help reshape the protein’s free energy landscape during activation. Our study highlights hydration water as an active medium with the capacity to drive long-range conformational changes underlying protein mechanics and offers a new conceptual understanding for engineering externally controllable protein actuators for biomedical studies to smart materials.

UR - https://doi.org/10.1101/2025.06.19.660617

U2 - 10.1101/2025.06.19.660617

DO - 10.1101/2025.06.19.660617

M3 - Preprint

C2 - 40667302

BT - Hydraulic Activation of the AsLOV2 photoreceptor

PB - BioRxiv

ER -