Entropically driven self-assembly of Lysinibacillus sphaericus S-layer proteins analyzed under various environmental conditions.

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 Biosci

authors

Teixeira LM,Strickland A,Mark SS,Bergkvist M,Sierra-Sastre Y,Batt CA

doi

10.1002/mabi.200900175

subject

Has Abstract

pub_date

2010-02-11 00:00:00

pages

147-55

issue

2

eissn

1616-5187

issn

1616-5195

journal_volume

10

pub_type

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