Frequency-Dependent Structural Responses of Amyloid-β Fibrils to Terahertz Pulses: A Nonequilibrium Molecular Dynamics Study

Nonequilibrium molecular dynamics shows that terahertz-to-mid-infrared pulses (0.5–60 THz) induce frequency-dependent losses of beta-sheet content in amyloid fibrils 2LMP, 2MXU, and 5OQV.

• Why it matters: Amyloid aggregation is linked to neurodegenerative diseases, yet it remains unclear how external terahertz/mid-infrared fields reshape fibril structure across pulse frequency and field strength.
• What they did: NEMD simulations applied intense pulses to three fibrils while scanning frequency from 0.5 to 60 THz in 0.5 THz steps, and compared secondary-structure and hydrogen-bond changes at 2, 23, 33, and 50 THz versus high-temperature controls.
• The result: Hydrogen-bond counts partially recover while interchain hydrogen bonds continue to decrease, and the authors propose a two-threshold electric-field framework (Eth1 onset, Eth2 persistent loss) to characterize disruption, pending validation of mechanisms and long-term recovery.

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