X-ray reflectivity and grazing incidence diffraction studies of interaction between human adhesion/growth-regulatory galectin-1 and DPPE—GM1 lipid monolayer at an air/water interface

被引:0
|
作者
J. Majewski
S. André
E. Jones
E. Chi
H.-J. Gabius
机构
[1] Los Alamos National Laboratory,Neutron Scattering Center, Los Alamos Neutron Science Center
[2] Ludwig-Maximilians-University Munich,Institute of Physiological Chemistry, Faculty of Veterinary Medicine
[3] University of New Mexico,Department of Chemical and Biological Engineering, Center for Biomedical Engineering
来源
Biochemistry (Moscow) | 2015年 / 80卷
关键词
agglutinin; Bragg peaks; ganglioside; lectin; X-ray diffraction/reflectivity;
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学科分类号
摘要
The specific interaction of ganglioside GM1 with the homodimeric (prototype) endogenous lectin galectin-1 triggers growth regulation in tumor and activated effector T cells. This proven biorelevance directed interest to studying association of the lectin to a model surface, i.e. a 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine/ganglioside GM1 (80: 20 mol%) monolayer, at a bioeffective concentration. Surface expansion by the lectin insertion was detected at a surface pressure of 20 mN/m. On combining the methods of grazing incidence X-ray diffraction and X-ray reflectivity, a transient decrease in lipid-ordered phase of the monolayer was observed. The measured electron density distribution indicated that galectin-1 is oriented with its long axis in the surface plane, ideal for cis-crosslinking. The data reveal a conspicuous difference to the way the pentameric lectin part of the cholera toxin, another GM1-specific lectin, is bound to the monolayer. They also encourage further efforts to monitor effects of structurally different members of the galectin family such as the functionally antagonistic chimera-type galectin-3.
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页码:943 / 956
页数:13
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