The transformation of the cellular prion protein (PrP(C)) into the infectious form (PrP(Sc)) is implicated in the invariably fatal transmissible spongiform encephalopathies. To identify a mechanism to prevent the undesired PrP(C)-->PrP(Sc) transformation, we investigated the interactions of recombinant prion proteins with a number of potential therapeutic agents which inhibit the PrP(Sc) formation, infectivity, and the accumulation of the misfolded form. We show that the prion aggregates formed in the presence of six compounds have no beta-structure, which is typical of the infectious form, and possess considerably higher alpha-helical content than the normal PrP(C). The investigated compounds stimulate the formation of alpha-helices and the destruction of beta-structure. They prevent the transformation of alpha-helical structure into beta-sheets. Probably, this is the reason for the resistance to PrP(C)-->PrP(Sc) transformation in the presence of these compounds. The results may be useful for the future therapy of neurodegenerative diseases.
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http://dx.doi.org/10.1016/j.bbrc.2006.03.135 | DOI Listing |
AAPS PharmSciTech
January 2025
Unidad de Investigación y Desarrollo, Probiomed S.A. de C.V, C. P. 52400, Tenancingo, Estado de México, México.
The available literature indicates that amino acids can stabilize proteins. Our experimental data demonstrated that lysine and glutamic acid can stabilize recombinant human erythropoietin (rhEPO) at 40°C for at least 1 month, as measured by RP-UPLC. Studies with different excipient concentrations demonstrated optimal concentrations of these amino acids within 10-12 mM.
View Article and Find Full Text PDFVet Res
January 2025
Engineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of Education, Chengdu, 611130, China.
In herpesvirus, the terminase subunit pUL15 is involved in cleavage of the viral genome concatemers in the nucleus. Previous studies have shown that herpes simplex virus 1 (HSV-1) pUL15 can enter the nucleus without other viral proteins and help other terminase subunits enter the nucleus. However, this study revealed that duck plague virus (DPV) pUL15 cannot localize independently to the nucleus and can only be localized in the nucleus in the presence of pUL28 and pUL33.
View Article and Find Full Text PDFJ Exp Clin Cancer Res
January 2025
Department of Medical and Surgical Sciences, Medical Oncology , Fondazione Policlinico Universitario "Agostino Gemelli" IRCCS, Rome, Italy.
Background: Pancreatic ductal adenocarcinoma (PDAC) is one of the most aggressive and deadly type of cancer, with an extremely low five-year overall survival rate. To date, current treatment options primarily involve various chemotherapies, which often prove ineffective and are associated with substantial toxicity. Furthermore, immunotherapies utilizing checkpoint inhibitors have shown limited efficacy in this context, highlighting an urgent need for novel therapeutic strategies.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Department of Physics, School of Physics and Information Engineering, Fuzhou University, Fuzhou 350108, P. R. China.
Perovskite quantum dots (PQDs) have attracted more and more attention in light-emitting diode (LED) devices due to their outstanding photoelectric properties. Surface ligands not only enable size control of quantum dots but also enhance their optoelectronic performance. However, the efficiency of exciton recombination in PQDs is often hindered by the desorption dynamics of surface ligands, leading to suboptimal electrical performance.
View Article and Find Full Text PDFViruses
December 2024
School of Medicine, Zhejiang University, Hangzhou 310063, China.
The Junín virus (JUNV) is one of the New World arenaviruses that cause severe hemorrhagic fever. Human transferrin receptor 1 (hTfR1) has been identified as the main receptor for JUNV for virus entry into host cells. To date, no treatment has been approved for JUNV.
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