Work

Nanoscopic surfactant behavior of the porin MspA in aqueous media

Year: 2013

Type: article

Abstract: The mycobacterial porin MspA is one of the most stable channel proteins known to date. MspA forms vesicles at low concentrations in aqueous buffers. Evidence from dynamic light scattering, transmission electron microscopy and zeta-potential measurements by electrophoretic light scattering indicate that MspA behaves like a nanoscale surfactant. The extreme thermostability of MspA allows these investigations to be carried out at temperatures as high as 343 K, at which most other proteins would quickly denature. The principles of vesicle formation of MspA as a function of temperature and the underlying thermodynamic factors are discussed here. The results obtained provide crucial evidence in support of the hypothesis that, during vesicle formation, nanoscopic surfactant molecules, such as MspA, deviate from the principles underlined in classical surface chemistry.

Source: Beilstein Journal of Nanotechnology

DOI: 10.3762/bjnano.4.30

Authors: Ayomi S Perera, Hongwang Wang, Tej B Shrestha, Deryl L Troyer, Stefan H Bossmann

Institution: Kansas State University

Language: English

Topic: Surfactants and Colloidal Systems

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: diamond

Funder: National Science Foundation

Award: Phase VI: Climate Change and Energy: Basic Science, Impacts, and Mitigation