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Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine.
|Title||Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Fu Y, Li B, Huang Z, Li Y, Yang Y|
|Journal||Langmuir : the ACS journal of surfaces and colloids|
|Date Published||2013 May 21|
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.