On the nature and role of water structuring in the adsorption of nonionic surfactants on hydrophobic surfaces

2007 ◽  
pp. 75-83 ◽  
Author(s):  
B. Kronberg ◽  
R. Silveston
Keyword(s):  
Nonionic Surfactants ◽  
Hydrophobic Surfaces ◽  
Water Structuring

Understanding the Role of Nonionic Surfactants during Catalysis in Microemulsion Systems on the Example of Rhodium-Catalyzed Hydroformylation

2017 ◽  
Vol 56 (36) ◽  
pp. 9934-9941 ◽  
Author(s):  
Tobias Pogrzeba ◽  
Marcel Schmidt ◽  
Natasa Milojevic ◽  
Carolina Urban ◽  
Markus Illner ◽  
...  
Keyword(s):  
Nonionic Surfactants

Competitive Adsorption of Monoclonal Antibodies and Nonionic Surfactants at Solid Hydrophobic Surfaces

2015 ◽  
Vol 104 (2) ◽  
pp. 593-601 ◽  
Author(s):  
Sebastian J. Kapp ◽  
Iben Larsson ◽  
Marco Van De Weert ◽  
Marité Cárdenas ◽  
Lene Jorgensen
Keyword(s):  
Monoclonal Antibodies ◽  
Nonionic Surfactants ◽  
Competitive Adsorption ◽  
Hydrophobic Surfaces

scholarly journals Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus

2020 ◽  
Vol 94 (15) ◽  
Author(s):  
Zhao-Xi Wang ◽  
Shu-Bo Liu ◽  
Hongxin Guan ◽  
Long-Feng Lu ◽  
Jia-Gang Tu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Oligomeric State ◽  
Hydrophobic Surfaces ◽  
Central Domain ◽  
P Protein ◽  
Homologous Virus ◽  
Β Sheets ◽  
P Proteins

ABSTRACT Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus in the common carp. The phosphoprotein (P protein) of SVCV is a multifunctional protein that acts as a polymerase cofactor and an antagonist of cellular interferon (IFN) response. Here, we report the 1.5-Å-resolution crystal structure of the P protein central domain (PCD) of SVCV (SVCVPCD). The PCD monomer consists of two β sheets, an α helix, and another two β sheets. Two PCD monomers pack together through their hydrophobic surfaces to form a dimer. The mutations of residues on the hydrophobic surfaces of PCD disrupt the dimer formation to different degrees and affect the expression of host IFN consistently. Therefore, the oligomeric state formation of the P protein of SVCV is an important mechanism to negatively regulate host IFN response. IMPORTANCE SVCV can cause spring viremia of carp with up to 90% lethality, and it is the homologous virus of the notorious vesicular stomatitis virus (VSV). There are currently no drugs that effectively cure this disease. P proteins of negative-strand RNA viruses (NSVs) play an essential role in many steps during the replication cycle and an additional role in immunosuppression as a cofactor. All P proteins of NSVs are oligomeric, but the studies on the role of this oligomerization mainly focus on the process of virus transcription or replication, and there are few studies on the role of PCD in immunosuppression. Here, we present the crystal structure of SVCVPCD. A new mechanism of immune evasion is clarified by exploring the relationship between SVCVPCD and host IFN response from a structural biology point of view. These findings may provide more accurate target sites for drug design against SVCV and provide new insights into the function of NSVPCD.

scholarly journals Role of Nonionic Surfactants on Adhesive Forces between Surfaces in Moist Cyclohexane.

2002 ◽  
Vol 39 (2) ◽  
pp. 96-101
Author(s):  
Yoichi Kanda ◽  
Yoshinori Nishitani ◽  
Ko Higashitani
Keyword(s):  
Nonionic Surfactants ◽  
Adhesive Forces
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