Hierarchical self-assembly of a collagen mimetic peptide (PKG)<italic>n</italic>(POG)2<italic>n</italic>(DOG)<italic>n</italic> via electrostatic interactions

doi:10.1007/s11706-011-0121-9

Front Mater Sci

2011, Vol. 5

Issue (3) : 293-300 https://doi.org/10.1007/s11706-011-0121-9

RESEARCH ARTICLE

Hierarchical self-assembly of a collagen mimetic peptide (PKG)_n(POG)₂_n(DOG)_n via electrostatic interactions

Ying SHI, Song WANG, Xiu-Mei WANG, Qiang CAI(

), Fu-Zhai CUI, Heng-De LI

Department of Materials Science and Engineering, Tsinghua University, Beijing 100084, China

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Abstract

A new type of collagen mimetic peptide, (PKG)_n(POG)₂_n(DOG)_n, with charged-domain ends had been designed and successfully prepared in this work, which self-assembled into collagen-like triple helices homotrimers. The collagen-like homotrimers underwent higher level of self-assembly via static electrical interaction between positive and negative domains. Transmission electron microscope (TEM) examinations showed three typical morphologies of homotrimer assembly, which were defined as film, bicontinuous and fibril morphology in this paper. The film was formed in the initial stage and gradually transformed to bicontinuous or fibril morphology to improve stability of the assemblies or decrease surface energy. Furthermore, mechanism of assembly process was proposed based on TEM observations and theoretical analyses of packing equation.

Keywords collagen mimetic peptide assembly morphology

Corresponding Author(s): CAI Qiang,Email:caiqiang@mail.tsinghua.edu.cn

Issue Date: 05 September 2011

Cite this article:

Ying SHI,Song WANG,Xiu-Mei WANG, et al. Hierarchical self-assembly of a collagen mimetic peptide (PKG)_n(POG)₂_n(DOG)_n via electrostatic interactions[J]. Front Mater Sci, 2011, 5(3): 293-300.

URL:

https://academic.hep.com.cn/foms/EN/10.1007/s11706-011-0121-9
https://academic.hep.com.cn/foms/EN/Y2011/V5/I3/293

Fig.1 Collagen mimetic peptide and its triple-helical structure: amino acid sequence of 12 and 24 amino acid peptide; triple-helical homotrimers of peptide chains.

Fig.2 Circular dichroism (CD) spectra to verify formation of the triple-helical structure of the synthesized peptide: 12 amino acid peptide without preheating; 24 amino acid peptide without preheating; 12 amino acid peptide after preheating; 24 amino acid peptide after preheating.

Fig.3 TEM photograph of peptide self-assemblies morphology: Bicontinuous morphology of 12 amino acid peptide; Bicontinuous morphology of 24 amino acid peptide, inserting a sketch of orthogonal bicontinuous morphology; Film morphology of 12 amino acid peptide after one-week incubation; Fibril morphology of peptide assembly; Formation of fibril morphology by film curling.

Fig.4 Sketches of peptide homotrimers assembling to film and fibril morphology: sketch of triple-helical homotrimer unit assembling to film morphology, inserting the film morphology observed by TEM; sketch of the film structure curling to fibrils, inserting the fibril morphology observed by TEM.

Fig.5 Formation of micro fibers of 12 and 24 amino acid peptide assembly under TEM.

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