Abstract:
: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.
journal_name
Macromol Bioscijournal_title
Macromolecular bioscienceauthors
Teixeira LM,Strickland A,Mark SS,Bergkvist M,Sierra-Sastre Y,Batt CAdoi
10.1002/mabi.200900175subject
Has Abstractpub_date
2010-02-11 00:00:00pages
147-55issue
2eissn
1616-5187issn
1616-5195journal_volume
10pub_type
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