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Authors = Tippawan Pissawong

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26 pages, 2920 KiB  
Article
Cell Penetrable Human scFv Specific to Middle Domain of Matrix Protein-1 Protects Mice from Lethal Influenza
by Fonthip Dong-din-on, Thaweesak Songserm, Tippawan Pissawong, Potjanee Srimanote, Jeeraphong Thanongsaksrikul, Kanyarat Thueng-in, Pattra Moonjit, Preeda Lertwatcharasarakul, Watee Seesuay and Wanpen Chaicumpa
Viruses 2015, 7(1), 154-179; https://doi.org/10.3390/v7010154 - 14 Jan 2015
Cited by 8 | Viewed by 6633
Abstract
A new anti-influenza remedy that can tolerate the virus antigenic variation is needed. Influenza virus matrix protein-1 (M1) is highly conserved and pivotal for the virus replication cycle: virus uncoating, assembly and budding. An agent that blocks the M1 functions should be an [...] Read more.
A new anti-influenza remedy that can tolerate the virus antigenic variation is needed. Influenza virus matrix protein-1 (M1) is highly conserved and pivotal for the virus replication cycle: virus uncoating, assembly and budding. An agent that blocks the M1 functions should be an effective anti-influenza agent. In this study, human scFv that bound to recombinant M1 middle domain (MD) and native M1 of A/H5N1 was produced. Phage mimotope search and computerized molecular docking revealed that the scFv bound to the MD conformational epitope formed by juxtaposed helices 7 and 9 of the M1. The scFv was linked molecularly to a cell penetrable peptide, penetratin (PEN). The PEN-scFv (transbody), when used to treat the cells pre-infected with the heterologous clade/subclade A/H5N1 reduced the viral mRNA intracellularly and in the cell culture fluids. The transbody mitigated symptom severity and lung histopathology of the H5N1 infected mice and caused reduction of virus antigen in the tissues as well as extricated the animals from the lethal challenge in a dose dependent manner. The transbody specific to the M1 MD, either alone or in combination with the cognate human scFvs specific to other influenza virus proteins, should be an effective, safe and mutation tolerable anti-influenza agent. Full article
(This article belongs to the Section Viral Immunology, Vaccines, and Antivirals)
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18 pages, 737 KiB  
Article
Synthesis and Theoretical Study of Molecularly Imprinted Nanospheres for Recognition of Tocopherols
by Theeraphon Piacham, Chanin Nantasenamat, Thummaruk Suksrichavalit, Charoenchai Puttipanyalears, Tippawan Pissawong, Supanee Maneewas, Chartchalerm Isarankura-Na-Ayudhya and Virapong Prachayasittikul
Molecules 2009, 14(8), 2985-3002; https://doi.org/10.3390/molecules14082985 - 12 Aug 2009
Cited by 42 | Viewed by 15566
Abstract
Molecular imprinting is a technology that facilitates the production of artificial receptors toward compounds of interest. The molecularly imprinted polymers act as artificial antibodies, artificial receptors, or artificial enzymes with the added benefit over their biological counterparts of being highly durable. In this [...] Read more.
Molecular imprinting is a technology that facilitates the production of artificial receptors toward compounds of interest. The molecularly imprinted polymers act as artificial antibodies, artificial receptors, or artificial enzymes with the added benefit over their biological counterparts of being highly durable. In this study, we prepared molecularly imprinted polymers for the purpose of binding specifically to tocopherol (vitamin E) and its derivative, tocopherol acetate. Binding of the imprinted polymers to the template was found to be two times greater than that of the control, non-imprinted polymers, when using only 10 mg of polymers. Optimization of the rebinding solvent indicated that ethanol-water at a molar ratio of 6:4 (v/v) was the best solvent system as it enhanced the rebinding performance of the imprinted polymers toward both tocopherol and tocopherol acetate with a binding capacity of approximately 2 mg/g of polymer. Furthermore, imprinted nanospheres against tocopherol was successfully prepared by precipitation polymerization with ethanol-water at a molar ratio of 8:2 (v/v) as the optimal rebinding solvent. Computer simulation was also performed to provide mechanistic insights on the binding mode of template-monomer complexes. Such polymers show high potential for industrial and medical applications, particularly for selective separation of tocopherol and derivatives. Full article
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