Chiral phonons are concerted mirror-symmetric movements of atomic groups connected by covalent and intermolecular bonds. Such lattice vibrations in crystals of biomolecules should be highly specific to their short- and long-range organizations, but their chiroptical signatures and structure–property relationships remain uncertain. Here we show that terahertz chiroptical spectroscopy enables the registration and attribution of chiral phonons for microscale and nanoscale crystals of amino acids and peptides. Theoretical analysis and computer simulations indicate that sharp mirror-symmetric bands observed for left- and right-handed enantiomers originate from the collective vibrations of biomolecules interconnected by hydrogen bonds into helical chains. The sensitivity of chiral phonons to minute structural changes can be used to identify physical and chemical differences in seemingly identical formulations of dipeptides used in health supplements. The generality of these findings is demonstrated by chiral phonons observed for amyloid nanofibrils of insulin. Their spectral signatures and polarization rotation strongly depend on their maturation stage, which opens a new door for medical applications of terahertz photonics.

手性声子是通过共价键和分子间键连接的原子团的镜像对称运动。生物分子晶体中的这种晶格振动对于它们的短程和长程组织应该是高度特异性的，但它们的手性特征和结构-性质关系仍然不确定。在这里，我们展示了太赫兹手性光谱能够对氨基酸和肽的微尺度和纳米尺度晶体的手性声子进行注册和归属。理论分析和计算机模拟表明，左旋和右旋对映异构体观察到的尖锐镜像对称带源于通过氢键互连成螺旋链的生物分子的集体振动。手性声子对微小结构变化的敏感性可用于识别保健品中看似相同的二肽配方中的物理和化学差异。这些发现的普遍性通过在胰岛素的淀粉样纳米纤维中观察到的手性声子得到证实。它们的光谱特征和偏振旋转很大程度上取决于它们的成熟阶段，这为太赫兹光子学的医学应用打开了一扇新的大门。