Structural and Spectroscopic Characterization of a Histidine-Containing Tetrapeptide Crystallized with Copper Chloride.

ABSTRACT: 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 a-axis. In contrast, the copper-containing crystals adopted a needle-like form with a distinct molecular orientation. Raman spectroscopy revealed coordination between h

SUBMITTER: Nishiyama Y 

PROVIDER: S-EPMC12268440 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature