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Updated: Aug 2, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Molecular Assembly and Gelating Behavior of (l)-Alanine Derivatives
Takahiro Soeta1, Shota Kurobe1, Yutaro Nirei1
1Division of Material Chemistry, Graduate School of Natural Science and Technology, Kanazawa University Kakuma, Kanazawa, Ishikawa, 920-1192, Japan.
Abstract:
In this study, a low-molecular-weight organogelator derived from (l)-amino acids was designed and synthesized. Gelation assays using (l)-amino acid derivatives were performed to confirm the gelation ability, which was found to be high in several compounds. The (l)-alanine derivatives were determined to be excellent gelators, forming good gels even when smaller amounts were added. These results led to a library of amino acid-derived organogelators. In addition, the thermal properties of the (l)-alanine derivatives with high gelation performance were measured. Differential scanning calorimetry measurements revealed that the thermal stability of the gels could be controlled by changing the gelator concentration. The surface states of the obtained gels were observed by field-emission scanning electron microscopy and atomic force microscopy measurements, which confirmed the structure of the self-molecular aggregates. Self-molecular aggregates were observed to be helical or sheet-like, and the gels were constructed by forming aggregates by self-molecular recognition.
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