Premium
Entropically Driven Self‐Assembly of Lysinibacillus sphaericus S‐Layer Proteins Analyzed Under Various Environmental Conditions
Author(s) -
Teixeira Leonardo Maestri,
Strickland Aaron,
Mark Sonny S.,
Bergkvist Magnus,
SierraSastre Yajaira,
Batt Carl A.
Publication year - 2010
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200900175
Subject(s) - monomer , chemistry , self assembly , enthalpy , kinetics , sodium , chemical engineering , entropy (arrow of time) , molecule , organic chemistry , polymer , thermodynamics , physics , quantum mechanics , engineering
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.