Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin

被引:39
作者
Dutta, Naba K. [1 ]
Choudhury, Namita R. [1 ]
Truong, My Y. [1 ]
Kim, Misook [2 ]
Elvin, Christopher M. [2 ]
Hill, Anita J. [3 ]
机构
[1] Univ S Australia, Ian Wark Res Inst, ARC Special Res Ctr, Adelaide, SA 5095, Australia
[2] CSIRO Livestock Ind, St Lucia, Qld 4067, Australia
[3] CSIRO Mat Sci & Engn, Clayton, Vic, Australia
基金
澳大利亚研究理事会;
关键词
Biomimetic; Rec1-resilin; Adsorption; Hydrophobicity; Scanning thermal microscopy; Nanostructure; ATOMIC-FORCE MICROSCOPY; DIP-PEN NANOLITHOGRAPHY; RUBBER-LIKE PROTEIN; ADSORPTION; ASSEMBLIES; MORPHOLOGY; PEPTIDES; SURFACES; ARRAYS; LAYER;
D O I
10.1016/j.biomaterials.2009.06.019
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Protein adsorption on surfaces is a fundamental step in many applications. While various methods such as lithography, self assembly using nanoparticles, layer-by-layer attachment, etc. have been employed, here we report fabrication of controlled nanostructure of a new resilin-mimetic elastic protein rec1-resilin using physical approaches. We investigate the assembly, morphology and tunability of the nanostructure of adsorbed rec1-resilin architectures by atomic force microscopy (AFM) and scanning thermal microscopy (SThm) demonstrating that the protein conformation and structure during assembly can be controlled by tuning the physical conditions at the surface. Our findings show distinct morphology and height of monomolecular rec1-resilin film, dependent on substrate surface energy. We also show that these heights, a function of molecular orientation, can be maintained on swelling and drying. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4868 / 4876
页数:9
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