Structural study of surfactant-dependent interaction with protein

Journal Article · Wed Jun 24 00:00:00 EDT 2015 · AIP Conference Proceedings

DOI:https://doi.org/10.1063/1.4917622· OSTI ID:22490208

Mehan, Sumit; Kohlbrecher, Joachim ^[1]

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1. Laboratory for Neutron Scattering, Paul Scherrer Institut, CH-5232 PSI Villigen (Switzerland)

Small-angle neutron scattering (SANS) has been used to study the complex structure of anionic BSA protein with three different (cationic DTAB, anionic SDS and non-ionic C12E10) surfactants. These systems form very different surfactant-dependent complexes. We show that the structure of protein-surfactant complex is initiated by the site-specific electrostatic interaction between the components, followed by the hydrophobic interaction at high surfactant concentrations. It is also found that hydrophobic interaction is preferred over the electrostatic interaction in deciding the resultant structure of protein-surfactant complexes.

• OSTI ID: 22490208
• Journal Information: AIP Conference Proceedings, Vol. 1665, Issue 1; Conference: 59. DAE solid state physics symposium 2014, Tamilnadu (India), 16-20 Dec 2014; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); ISSN 0094-243X
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ABUNDANCE
CONCENTRATION RATIO
ELECTROSTATICS
NEUTRON DIFFRACTION
PROTEINS
SMALL ANGLE SCATTERING
SURFACTANTS