水素分子がペプシンの酵素活性および構造特性に与える影響：in vitro解析
Using pepsin as a model protein, this in vitro study examined how hydrogen-rich water influences enzymatic activity and structural properties. Enzymatic assays, atomic force microscopy-based peakforce quantitative nanomechanical mapping (PF-QNM), and terahertz time-domain spectroscopy (THz-TDS) were employed. Results showed that hydrogen-rich water elevated pepsin activity and apparent molecular height while modifying mechanical properties (Young's modulus) and terahertz dynamics. These findings point to a mechanism in which hydrogen molecules interact with pepsin through localized alterations at hydrophobic interfaces within the protein. The study provides initial biophysical evidence for a direct interaction between molecular hydrogen and proteins, offering mechanistic insight into how dissolved hydrogen and other gases may exert biological effects.
Molecular hydrogen is proposed to interact with pepsin by inducing localized changes at hydrophobic interfaces within the protein, leading to increased enzymatic activity and alterations in Young's modulus and terahertz dynamics.
This is basic research at the cellular or molecular level. For human application, inhalation is the most promising delivery route, but inhalation carries explosion risk and concentration matters (empirical LFL of 10%; high-concentration devices are not recommended).
See also:
https://h2-papers.org/en/papers/32087530