LIPSS enables in situSANS 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 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 image above1. LIPSS was designed for low viscosity solutions and its performance depends on the specific environment required. If you are interested in using LIPSS it is strongly recommended that you discuss measurement needs in advance with Susana Teixeira [scm5(at)nist.gov] .
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
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
S. Teixeira et al., High Pressure Cell for Bio-SANS Studies Under Sub-zero Temperatures or Heat Denaturing Conditions’. J. Neutron Res20,13 – 23 (2018).
L. He et al., Conformational changes in Sindbis virus induced by decreased pH are revealed by small-angle neutron scattering. J Virol86, 1982-1987 (2012)
C. Dias et al., The hydrophobic effect and its role in cold denaturation, Cryobiology60 ,91–99 (2010).
K. Lazar et al., Cold denaturation of monoclonal antibodies. mAbs2, 42 - 52 (2010).
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 Science14(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).
BL2 Biomolecular Labeling Laboratory: supports labeling proteins and nucleic acids with 2H, 13C and 15N. It also has the capability for domain labeling and amino acid-specific labeling of proteins expressed in bacteria and yeast.
SASSIE program suite to generate and manipulate large numbers of structures and to calculate the SANS, SAXS, and neutron reflectivity profiles from atomistic structures. Includes a Biomolecular Scattering Length density calculator.
Sasview: small angle scattering data analysis software package