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Journal of Nanomaterials
Volume 2014, Article ID 241975, 7 pages
Research Article

Structure and Identification of Solenin: A Novel Fibrous Protein from Bivalve Solen grandis Ligament

1College of Pharmacy, Guangxi Medical University, 22 Shuangyong Road, Nanning, Guangxi 530021, China
2College of Materials Science and Engineering, Guangxi University, 100 Daxue Road, Nanning, Guangxi 530004, China

Received 19 May 2014; Accepted 17 June 2014; Published 8 July 2014

Academic Editor: Jingxia Wang

Copyright © 2014 Jun Meng et al. 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.


Fibrous proteins, which derived from natural sources, have been acting as templates for the production of new materials for decades, and most of them have been modified to improve mechanical performance. Insight into the structures of fibrous proteins is a key step for fabricating of bioinspired materials. Here, we revealed the microstructure of a novel fibrous protein: solenin from Solen grandis ligament and identified the protein by MALDI-TOF-TOF-MS and LC-MS-MS analyses. We found that the protein fiber has no hierarchical structure and is homologous to keratin type II cytoskeletal 1 and type I cytoskeletal 9-like, containing “SGGG,” “SYGSGGG,” “GS,” and “GSS” repeat sequences. Secondary structure analysis by FTIR shows that solenin is composed of 41.8% β-sheet, 16.2% β-turn, 26.5% α-helix, and 9.8% disordered structure. We believe that the β-sheet structure and those repeat sequences which form “glycine loops” may give solenin excellence elastic and flexible properties to withstand tensile stress caused by repeating opening and closing of the shell valves in vivo. This paper contributes a novel fibrous protein for the protein materials world.