Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin.
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.
Dutta
Naba K
NK
Ian Wark Research Institute, ARC Special Research Centre, Mawson Lakes Campus, University of South Australia, Mawson Lakes, Adelaide, SA 5095, Australia. naba.dutta@unisa.edu.au
Choudhury
Namita R
NR
Truong
My Y
MY
Kim
Misook
M
Elvin
Christopher M
CM
Hill
Anita J
AJ
D000327:Adsorption; D000818:Animals; D003432:Cross-Linking Reagents; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D019476:Insect Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D036103:Nanotechnology; D011487:Protein Conformation; D012825:Silicon / Q000737:chemistry; D013499:Surface Properties; D014867:Water / Q000737:chemistry
D003432:Cross-Linking Reagents; D029721:Drosophila Proteins; D019476:Insect Proteins; D014867:Water; C030951:resilin; D012825:Silicon