Nishiyama Yumie, Dimo Vanessa Seudo, Motai Kazunori, Wada Yuki, Kawano Masaki, Hayamizu Yuhei
Department of Materials Science and Engineering, School of Materials and Chemical Technology, Institute of Science Tokyo, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan.
Department of Chemistry, School of Science, Institute of Science Tokyo, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan.
ACS Omega. 2025 Jul 4;10(27):29647-29653. doi: 10.1021/acsomega.5c03327. eCollection 2025 Jul 15.
Metal coordination has emerged as a promising strategy to modulate peptide self-assembly and enhance crystal stability. In this study, we investigated the crystallization behavior of a histidine-containing tetrapeptide in the presence and absence of copper ions to elucidate the role of metal coordination in peptide assembly. Crystals were obtained under both conditions and characterized using single-crystal X-ray diffraction (sc-XRD) and angle-resolved polarized Raman spectroscopy. The copper-free crystals exhibited a rod-like morphology stabilized predominantly by hydrogen bonding, with molecular alignment along the -axis. In contrast, the copper-containing crystals adopted a needle-like form with a distinct molecular orientation. Raman spectroscopy revealed coordination between histidine side chains and copper ions, suggesting that metal binding modulates the intermolecular packing and alters the crystal architecture. These findings demonstrate how metal-peptide interactions influence peptide crystallization and highlight the utility of vibrational spectroscopy in probing such interactions at the molecular level.
金属配位已成为一种有前景的策略，可用于调节肽的自组装并增强晶体稳定性。在本研究中，我们研究了含组氨酸的四肽在有铜离子和无铜离子存在下的结晶行为，以阐明金属配位在肽组装中的作用。在两种条件下均获得了晶体，并使用单晶X射线衍射（sc-XRD）和角分辨偏振拉曼光谱对其进行了表征。不含铜的晶体呈现出主要由氢键稳定的棒状形态，分子沿轴排列。相比之下，含铜的晶体呈针状，具有独特的分子取向。拉曼光谱揭示了组氨酸侧链与铜离子之间的配位，表明金属结合调节了分子间堆积并改变了晶体结构。这些发现证明了金属-肽相互作用如何影响肽的结晶，并突出了振动光谱在分子水平探测此类相互作用中的实用性。
