Entropically driven self-assembly of Lysinibacillus sphaericus S-layer proteins analyzed under various environmental conditions.
S-Layer proteins are an example of bionanostructures that can be exploited in nanofabrication. In addition to their ordered structure, the ability to self-assembly is a key feature that makes them a promising technological tool. Here, in vitro self-assembly kinetics of SpbA was investigated, and found that it occurs at a rate that is dependent on temperature, its concentration, and the concentration of calcium ions and sodium chloride. The activation enthalpy (120.81 kJ . mol(-1)) and entropy (129.34 J . mol(-1) . K(-1)) obtained infers that the incorporation of monomers incurs in a net loss of hydrophobic surface. By understanding how the protein monomers drive the self-assembly at different conditions, the rational optimization of this process was feasible.
Teixeira
Leonardo Maestri
LM
Department of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Strickland
Aaron
A
Mark
Sonny S
SS
Bergkvist
Magnus
M
Sierra-Sastre
Yajaira
Y
Batt
Carl A
CA
D001407:Bacillus / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D019277:Entropy; D004777:Environment; D007700:Kinetics; D008027:Light; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D046529:Microscopy, Electron, Transmission; D009004:Monosaccharide Transport Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D020836:Protein Structure, Quaternary; D012542:Scattering, Radiation; D013057:Spectrum Analysis; D013696:Temperature
D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; D009004:Monosaccharide Transport Proteins; C055764:S-layer proteins; C120455:SbpA protein, bacteria