TY - JOUR
T1 - Effect of red blood cell shape changes on haemoglobin interactions and dynamics
T2 - A neutron scattering study: Hb Interactions and Dynamics in RBCs
AU - Shou, Keyun
AU - Sarter, Mona
AU - De Souza, Nicolas R.
AU - De Campo, Liliana
AU - Whitten, Andrew E.
AU - Kuchel, Philip W.
AU - Garvey, Christopher J.
AU - Stadler, Andreas M.
PY - 2020
Y1 - 2020
N2 - By using a combination of experimental neutron scattering techniques, it is possible to obtain a statistical perspective on red blood cell (RBC) shape in suspensions, and the inter-relationship with protein interactions and dynamics inside the confinement of the cell membrane. In this study, we examined the ultrastructure of RBC and protein-protein interactions of haemoglobin (Hb) in them using ultra-small-angle neutron scattering and small-angle neutron scattering (SANS). In addition, we used the neutron backscattering method to access Hb motion on the ns time scale and Å length scale. Quasi-elastic neutron scattering (QENS) experiments were performed to measure diffusive motion of Hb in RBCs and in an RBC lysate. By using QENS, we probed both internal Hb dynamics and global protein diffusion, on the accessible time scale and length scale by QENS. Shape changes of RBCs and variation of intracellular Hb concentration were induced by addition of the Na + -selective ionophore monensin and the K + -selective one, valinomycin. The experimental SANS and QENS results are discussed within the framework of crowded protein solutions, where free motion of Hb is obstructed by mutual interactions.
AB - By using a combination of experimental neutron scattering techniques, it is possible to obtain a statistical perspective on red blood cell (RBC) shape in suspensions, and the inter-relationship with protein interactions and dynamics inside the confinement of the cell membrane. In this study, we examined the ultrastructure of RBC and protein-protein interactions of haemoglobin (Hb) in them using ultra-small-angle neutron scattering and small-angle neutron scattering (SANS). In addition, we used the neutron backscattering method to access Hb motion on the ns time scale and Å length scale. Quasi-elastic neutron scattering (QENS) experiments were performed to measure diffusive motion of Hb in RBCs and in an RBC lysate. By using QENS, we probed both internal Hb dynamics and global protein diffusion, on the accessible time scale and length scale by QENS. Shape changes of RBCs and variation of intracellular Hb concentration were induced by addition of the Na + -selective ionophore monensin and the K + -selective one, valinomycin. The experimental SANS and QENS results are discussed within the framework of crowded protein solutions, where free motion of Hb is obstructed by mutual interactions.
KW - haemoglobin
KW - protein diffusion
KW - protein interactions
KW - quasi-elastic neutron scattering
KW - red blood cells
KW - small-angle neutron scattering
U2 - 10.1098/rsos.201507rsos201507
DO - 10.1098/rsos.201507rsos201507
M3 - Article
AN - SCOPUS:85096304647
SN - 2054-5703
VL - 7
JO - Royal Society Open Science
JF - Royal Society Open Science
IS - 10
M1 - 201507
ER -