DOI > 10.5291/ILL-DATA.9-13-820

This proposal is publicly available since 07/28/2024

Title

Elucidating electrostatic and hydrophobic interactions in protein-surfactant systems using contrast variation SANS

Abstract

Liquid pharmaceutical formulations are commonly comprised of proteins and surfactants, which interact in solution in order to provide an increase in the system stability. Although these systems have been significantly investigated in the last few years, there is a lack of consensus concerning the interaction between proteins and surfactants. We believe that small-angle neutron scattering and contrast variation can provide specific information about these systems and contribute to resolve the puzzle. In this experiment we aim to elucidate the interactions between human growth hormone and different prototypical ionic amphiphiles at room temperature. The use of isotope labelling and contrast matching will provide detailed information of the different parts of the system, which will be co-refined in order to provide structural information of the protein-surfactant complexes.

Experimental Report

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Data Citation

The recommended format for citing this dataset in a research publication is in the following format:

Adrian Sanchez-Fernandez; Judith E. Houston; LEUNG Anna elizabeth; NYLANDER Tommy; OBIOLS RABASA Marc; PREVOST Sylvain; SJOGREN Helen; TERRY Ann; ULVENLUND Stefan and Marie Wahlgren. (2019). Elucidating electrostatic and hydrophobic interactions in protein-surfactant systems using contrast variation SANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-820

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Metadata

Experiment Parameters

  • Environment temperature

    25 C
  • Experiment moment

    0.004-0.5 Å-1
  • Experiment res moment

    dq/q = 9 %

Sample Parameters

  • Formula

    • Human growth hormone
    • C12H25SO4Na
    • C15H34Cl
    • Bovine Serum Albumin