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Controlled arrays of self-assembled peptide nanostructures in solution and at interface.
Wang, Jian-Xun; Lei, Qi; Luo, Guo-Feng; Cai, Teng-Teng; Li, Jiang-Lan; Cheng, Si-Xue; Zhuo, Ren-Xi; Zhang, Xian-Zheng.
Afiliação
  • Wang JX; Key Laboratory of Biomedical Polymers of Ministry of Education and Department of Chemistry, Wuhan University, Wuhan 430072, P R China.
Langmuir ; 29(23): 6996-7004, 2013 Jun 11.
Article em En | MEDLINE | ID: mdl-23663135
ABSTRACT
Controlling the formation of large and homogeneous arrays of bionanostructures through the self-assembly approach is still a great challenge. Here, we report the spontaneous formation of highly ordered arrays based on aligned peptide nanostructures in a solution as well as at an interface by self-assembly. By controlling the time and temperature of self-assembly in the solution, parallel fibrous alignments and more sophisticated two-dimensional "knitted" fibrous arrays could be formed from aligned rod-like fibers. During the formation of such arrays, the "disorder-to-order" transitions are controlled by the temperature-responsible motile short hydrophobic tails of the gemini-like amphiphilic peptides (GAPs) with asymmetric molecular conformation. In addition, the resulting long-range-ordered "knitted" fibrous arrays are able to direct mineralization of calcium phosphate to form organic-inorganic composite materials. In this study, the self-assembly behavior of these peptide building blocks at an interface was also studied. Highly ordered spatial arrays with vertically or horizontally aligned nanostructures such as nanofibers, microfibers, and microtubes could be formed through interfacial assembly. The regular structures and their alignments on the interface are controlled by the alkyl chain length of building blocks and the hydrophilicity/hydrophobicity property of the interface.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Nanoestruturas Idioma: En Ano de publicação: 2013 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Nanoestruturas Idioma: En Ano de publicação: 2013 Tipo de documento: Article