[22a-C106-1~11] 12.2 Characterization and Materials Physics

[22a-C106-3] Understanding the effect of the sequence order of tetrapeptide crystals on the crystal structure and the self-assembly process

〇(D)Kazunori Motai¹, Yuki Wada², Masaki Kawano², Yuhei Hayamizu¹ (1.Tokyo tech., 2.Tokyo tech Department of Science.)

Keywords:peptide, X-ray diffiraction, self-assembly

In this study, in order to investigate the effect of sequence order on self-assembly, we performed crystallization and single-crystal structure analysis of three tetrapeptides, including hydrophobic phenylalanine (F) and hydrophilic glutamic acid (E), as models. The three tetrapeptides were found to have a regular lattice pattern of dots on the hydrophobic and hydrophilic domains, and a two-dimensional layered pattern.