Proteins in a brave new surfactant world
This review discusses emerging topics within the field of protein–surfactant interactions over the last 4–5years. The application of small-angle x-ray scattering has allowed us to construct ever more detailed models of the structures of different protein–surfactant complexes and has revealed common...
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Published in | Current opinion in colloid & interface science Vol. 20; no. 3; pp. 161 - 169 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
01.06.2015
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Subjects | |
Online Access | Get full text |
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Summary: | This review discusses emerging topics within the field of protein–surfactant interactions over the last 4–5years. The application of small-angle x-ray scattering has allowed us to construct ever more detailed models of the structures of different protein–surfactant complexes and has revealed common features shared between electrophoretic protein–SDS complexes and liprotides (complexes between lipids and partially denatured proteins), namely a generic core-shell structure which can also form beads on a string. SDS emerges as the best surfactant for gel electrophoresis from a series of studies comparing it with surfactants differing in chain length, degree of branching, and fluorination, as well as dodecyl sulfate with different counterions. Nevertheless, these surfactants possess useful properties for alternative applications. SDS also continues to serve as a useful tool for systematic folding/unfolding studies of membrane proteins together with the non-ionic surfactant dodecyl maltoside, as well as for studying hyperstable kinetically trapped proteins. Biosurfactants are coming to the fore as sustainable alternatives to chemical surfactants and show unique properties toward proteins that combine aspects of both ionic and non-ionic surfactants.
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•SDS remains the most useful surfactant for SDS-PAGE and conformational trapping.•Counterions modulate dodecyl sulfate cmc and thus alter its denaturation range.•Fluorinated surfactants allow measurement of helix water-membrane transfer energies.•Biosurfactants are promising surfactant alternatives with novel properties.•SAXS/SANS provide new structural insights into protein–surfactant complexes. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1359-0294 1879-0399 |
DOI: | 10.1016/j.cocis.2015.07.003 |