title: Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine.
abstract: The organization of peptides and proteins attracts much attention, due to the biofunctionalities of the self-assemblies. Herein, four dipeptides derived from alanine were synthesized. It was found that the handedness of their self-assemblies was controlled by the chirality of the alanines at the terminals. The organic self-assemblies were studied using circular dichroism, (1)H NMR, Fourier transform infrared, field-emission electron microscopy, transmission electron microscopy, and X-ray diffraction. The results indicated that the electrostatic interactions among the carboxylate groups and H-bondings among the amide groups at the terminals play important roles in the formation of the organic self-assemblies.
authors.affiliation: Jiangsu Key Laboratory of Advanced Functional Polymer Design and Application, Department of Polymer Science and Engineering, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou, PR China.
authors.forename: Yitai
authors.initials: Y
authors.lastname: Fu
authors.forename: Baozong
authors.initials: B
authors.lastname: Li
authors.forename: Zhibin
authors.initials: Z
authors.lastname: Huang
authors.forename: Yi
authors.initials: Y
authors.lastname: Li
authors.forename: Yonggang
authors.initials: Y
authors.lastname: Yang
mesh_terms: D000409:Alanine / Q000737:chemistry*; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry; D008968:Molecular Conformation; D010316:Particle Size
chemical_list: D004151:Dipeptides; D000409:Alanine