Self-Assembly of Peptide-Containing Mesogens: Thermotropic Liquid-Crystalline Properties and Macroscopic Alignment of Amphiphilic Bioconjugates

• Published in: Bulletin of the Chemical Society of Japan Vol. 94; no. 5; pp. 1588 - 1593
• Main Authors: Eimura, Hiroki, Niwa, Anna, Uchida, Junya, Kato, Takashi
• Format: Journal Article
• Language: English
• Published: TOKYO The Chemical Society of Japan 15.05.2021; Chemical Soc Japan; Chemical Society of Japan
• Subjects: Aspartic acid; Chains; Chemistry; Chemistry, Multidisciplinary; Crystal structure; Crystallinity; Glycine; Hydrogen bonding; Hydrogen bonds; Liquid crystals; Peptides; Physical Sciences; Science & Technology; Self-assembly; Shearing; Thermal stability; Liquid crystal; Peptide; Self-assembly; DESIGN; ACID; LITHIUM SALT; ION CONDUCTORS; BUILDING-BLOCKS; SUPRAMOLECULAR CHIRALITY; HYDROGEN-BONDS; PHASE; TRANSPORT; DERIVATIVES
• ISSN: 0009-2673; 1348-0634
• DOI: 10.1246/bcsj.20210051

Thermotropic liquid crystals having tripeptide moieties are reported. A series of peptide chains including arginine-glycine-aspartic acid (RGD), glycine-glycine-aspartic acid (GGD), and triglycine (GGG) moieties is connected to a rigid-rod core through a flexible tetraoxyethylene spacer. These bioconjugated mesogens form intermolecular hydrogen bonds through amide groups in the tripeptide moieties. It is found that side chains in the tripeptide-conjugated mesogens constrain intermolecular hydrogen bonding in the bulk states, which affects the formation of the liquid-crystalline phases. The rigid-rod mesogens bearing RGD and GGD peptide sequence exhibit smectic phases with high thermal stability of the mesophases. The liquid-crystalline assemblies of the mesogen-containing peptides are macroscopically oriented by mechanical shearing. The present design of bioconjugated liquid crystals could lead to the development of new self-assembled materials for biological applications.