LIQUID INSERTION PRESSURE SYSTEM FOR SANS (LIPSS)
LIPSS enables in situ SANS measurements under broad ranges of pressure and temperature, so that sample environment effects can be probed from minutes to hours1. No radiation damage and an extended q-range make HP-SANS complementary to HP-SAXS measurements, providing information on a broad range of molecular sizes, shape, aggregation, folding/unfolding, etc. The non destructive nature of neutrons allows for hysteresis effects to be probed, while contrast variation SANS can be used to highlight contributions to scattering from specific components of complex macromolecular assemblies such as viruses2 or others.
LIPSS is a high-pressure (HP) system (see specifications below): the McHugh sample cell is made of a high-nickel-content austenitic steel and is capable of withstanding a maximum pressure up to 350 MPa (3.5 kbar). A Peltier system controls the temperature between -20°C and +65°C: under pressure, subzero temperatures can be accessed in the absence of ice. The sample is loaded through an injection system that minimizes air bubbles and fills the cell completely. A separator isolates the sample from the pressurizing medium, as shown schematically in the image1. LIPSS was designed for low viscosity solutions and its performance depends on the specific environment required. It is strongly recommended that you discuss measurement needs in advance, with Susana Teixeira [scm5(at)nist.gov] or your local contact.
Past and potential applications of HP-SANS and the LIPSS sample environment include studies on:
- cold denaturation of proteins3
- subzero temperature effects on storage of monoclonal antibodies4
- high-pressure low-temperature processing of food proteins5
- high-pressure response of amyloid folds6
- self-assembled lipid nanoparticles7
- viral inactivation8,9
- pressure-assisted enzymatic digestion of antibodies10
- protein aggregation under pressure11,12
- lipid phase transitions13
- surfactant self-assembly at high pressure14
- polymer blend nucleation and interactions15,16
- engineering baroplastic behavior of block copolymers17
Let us know about the sample environment you need
There are ongoing efforts at the NCNR to optimize the HP BioSANS system described above, namely through improved automation, thermal insulation and improved cooling/heating power. Contact Susana Teixeira to find out more, or discuss the specific needs of your experiment.
- S. Teixeira et al., High Pressure Cell for Bio-SANS Studies Under Sub-zero Temperatures or Heat Denaturing Conditions’. J. Neutron Res 20,13 – 23 (2018).
- L. He et al., Conformational changes in Sindbis virus induced by decreased pH are revealed by small-angle neutron scattering. J Virol 86, 1982-1987 (2012)
- C. Dias et al., The hydrophobic effect and its role in cold denaturation, Cryobiology 60 ,91–99 (2010).
- K. Lazar et al., Cold denaturation of monoclonal antibodies. mAbs 2, 42 - 52 (2010).
- S.C.M Teixeira. High-pressure small-angle neutron scattering for food studies, Curr. Op. Colloid & Interface Science 42, 99-109 (2019).
- J. Torrent et al., High pressure response of amyloid folds. Viruses 11(3): 202 (2019).
- C. Kulkarni et al., Effects of High Pressure on Internally Self-Assembled Lipid Nanoparticles: A Synchrotron Small-Angle X-ray Scattering (SAXS) Study. Langmuir 32, 45, 11907–11917 (2016).
Oliveira et al., Low Temperature and Pressure Stability of Picornaviruses: Implications for Virus Uncoating. Biophysical J. 76, 3, 1270-1279 (1999).
D. Kingsley. High Pressure Processing and its Application to the Challenge of Virus-Contaminated Foods. Food Environ Virol. 5(1): 1–12 (2013).
Fang et al. (2016) Pressurized online pepsin digestion of mAb IgG2 for Hydrogen Deuterium Exchange Mass Spectrometry. https://www.waters.com/webassets/cms/library/docs/720005693en.pdf. Accessed April 2020.
Jackson & McGillivray. Protein aggregate structure under high pressure. Chem. Commun. 47, 487–489 (2011).
Seefeldt et al., High-pressure studies of aggregation of recombinant human interleukin-1 receptor antagonist: Thermodynamics, kinetics, and application to accelerated formulation studies. Protein Science 14(9): 2258–2266 (2005).
Hammouda and Clover. SANS from P85/Water-d under Pressure. Langmuir 26(9), 6625–6629 (2010).
Leseman et al., Self-Assembly at High Pressures: SANS Study of the Effect of Pressure on Microstructure of C8E5 Micelles in Water. Ind. Eng. Chem. Res. 42, 6425-6430 (2003).
Patel et al., Observing Nucleation Close to the Binodal by Perturbing Metastable Polymer Blends. Macromol. 40(5), 1675 (2007).
Ruegg et al., Effect of Pressure on a Multicomponent A/B/A-C Polymer Blend with Attractive and Repulsive Interactions. Macromol. 40(2), 355 (2007).
Ruzette et al., Pressure effects on the phase behavior of styrene/n-alkyl methacrylate block copolymers. Macromol. 36(9), 3351 (2003).
Certain trade names and company products are mentioned in the text or identified. In no case does such identification imply recommendation or endorsement by the National Institute of Standards and Technology (NIST), nor does it imply that the products are necessarily the best available for the purpose.
By selecting almost any of these links, you will be leaving NIST webspace. We provide these links because they may have information of interest to you. No inferences should be drawn because some sites are referenced, or not, from this page. There may be other web sites that are more appropriate for your purpose. NIST does not necessarily endorse the views expressed, or concur with the assertions presented on these sites. Further, NIST does not endorse any commercial products that may be mentioned on these sites.