AI Article Synopsis

  • Surfactants SDS and CTAB interact differently with human serum albumin (HSA) on self-assembled monolayers (SAMs) of hydrophobic alkyl chains, with CTAB being more effective in HSA removal.
  • Despite rinsing, HSA remains on the surface after treatment with SDS, while CTAB completely removes it.
  • X-ray analysis shows that CTAB molecules stay interdigitated within the SAM, indicating stronger interaction with the surface compared to SDS.

Article Abstract

The surfactants sodium dodecyl sulfate (SDS) and cetyltrimethylammonium bromide (CTAB) displace human serum albumin (HSA) from loosely packed self-assembled monolayers (SAM) of hydrophobic alkyl chains by different means. Removal of HSA is of interest because previous work has suggested that the adsorption of HSA to such loosely packed SAMs may be sufficiently tenacious to offer opportunities for surface passivation. While HSA remains on the surface after exposure to SDS and rinsing, no protein remains after exposure to CTAB and rinsing. X-ray reflectivity and X-ray photoelectron spectroscopy measurements indicate that CTAB molecules remain interdigitated in the loosely packed SAM after rinsing, suggesting that CTAB is more effective in removing the HSA because it interacts more strongly with the SAM.

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http://dx.doi.org/10.1016/S0021-9797(03)00063-8DOI Listing

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