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Journal of Nanomaterials
Volume 2012 (2012), Article ID 537262, 9 pages
Research Article

Strategy for Designing Self-Assembling Peptides to Prepare Transparent Nanofiber Hydrogel at Neutral pH

1R & D Division, Applied Technology Development Department, Menicon Co., Ltd., 5-1-10 Takamoridai, Kasugai, Aichi 487-0032, Japan
2Department of Frontier Materials, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya 466-8555, Japan

Received 16 December 2011; Revised 6 March 2012; Accepted 7 March 2012

Academic Editor: Tong Lin

Copyright © 2012 Hidenori Yokoi and Takatoshi Kinoshita. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


This study examined the formation of nanofiber hydrogels at neutral pH for 16 types of peptides with different net charges, hydrophobicities, and degrees of polymerization. The peptides formed various hydrogels depending on the arrangement of charged amino acids in the antiparallel β-sheet structure. Circular dichroism (CD) measurement, atomic force microscopy (AFM), visible light spectroscopy, and dynamic viscoelasticity measurement showed that the formation of transparent nanofiber hydrogels in peptides requires at least 2 additional positively or negatively charged amino acids per peptide. When designing the amino acid sequence, it is important to consider both the net charge and position of the charged amino acids, and it should be ensured that basic amino acids do not face other basic ones in the antiparallel β-sheet structure. Peptides that had charged amino acids clustered at the center of the nanofiber formed rigid gels.