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  • 1
    Publication Date: 2018-08-26
    Description: Cancers, Vol. 10, Pages 289: miRNA-205 Nanoformulation Sensitizes Prostate Cancer Cells to Chemotherapy Cancers doi: 10.3390/cancers10090289 Authors: Prashanth K. B. Nagesh Pallabita Chowdhury Elham Hatami Vijaya K. N. Boya Vivek K. Kashyap Sheema Khan Bilal B. Hafeez Subhash C. Chauhan Meena Jaggi Murali M. Yallapu The therapeutic application of microRNA(s) in the field of cancer has generated significant attention in research. Previous studies have shown that miR-205 negatively regulates prostate cancer cell proliferation, metastasis, and drug resistance. However, the delivery of miR-205 is an unmet clinical need. Thus, the development of a viable nanoparticle platform to deliver miR-205 is highly sought. A novel magnetic nanoparticle (MNP)-based nanoplatform composed of an iron oxide core with poly(ethyleneimine)-poly(ethylene glycol) layer(s) was developed. An optimized nanoplatform composition was confirmed by examining the binding profiles of MNPs with miR-205 using agarose gel and fluorescence methods. The novel formulation was applied to prostate cancer cells for evaluating cellular uptake, miR-205 delivery, and anticancer, antimetastasis, and chemosensitization potentials against docetaxel treatment. The improved uptake and efficacy of formulations were studied with confocal imaging, flow cytometry, proliferation, clonogenicity, Western blot, q-RT-PCR, and chemosensitization assays. Our findings demonstrated that the miR-205 nanoplatform induces significant apoptosis and enhancing chemotherapeutic effects in prostate cancer cells. Overall, these study results provide a strong proof-of-concept for a novel nonviral-based nanoparticle protocol for effective microRNA delivery to prostate cancer cells.
    Electronic ISSN: 2072-6694
    Topics: Medicine
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  • 2
    Publication Date: 2012-09-18
    Description: Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3538848/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3538848/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekiert, Damian C -- Kashyap, Arun K -- Steel, John -- Rubrum, Adam -- Bhabha, Gira -- Khayat, Reza -- Lee, Jeong Hyun -- Dillon, Michael A -- O'Neil, Ryann E -- Faynboym, Aleksandr M -- Horowitz, Michael -- Horowitz, Lawrence -- Ward, Andrew B -- Palese, Peter -- Webby, Richard -- Lerner, Richard A -- Bhatt, Ramesh R -- Wilson, Ian A -- GM080209/GM/NIGMS NIH HHS/ -- HHSN266200700010C/PHS HHS/ -- P01 AI058113/AI/NIAID NIH HHS/ -- P01AI058113/AI/NIAID NIH HHS/ -- P41 RR017573/RR/NCRR NIH HHS/ -- T32 GM080209/GM/NIGMS NIH HHS/ -- U01 AI070373/AI/NIAID NIH HHS/ -- U01AI070373/AI/NIAID NIH HHS/ -- U54 GM094586/GM/NIGMS NIH HHS/ -- U54-AI057158/AI/NIAID NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- England -- Nature. 2012 Sep 27;489(7417):526-32. doi: 10.1038/nature11414. Epub 2012 Sep 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22982990" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Neutralizing/*chemistry/genetics/*immunology ; Antibodies, Viral/*chemistry/genetics/*immunology ; Antibody Specificity/genetics/*immunology ; Antigens, Viral/chemistry/immunology ; Binding Sites ; Complementarity Determining Regions/chemistry/genetics/immunology ; Conserved Sequence ; Cross Reactions/genetics/immunology ; Crystallography, X-Ray ; Enzyme-Linked Immunosorbent Assay ; Epitopes/chemistry/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/immunology ; Influenza A Virus, H1N1 Subtype/chemistry/immunology ; Influenza A Virus, H3N2 Subtype/chemistry/immunology ; Influenza A virus/chemistry/*classification/*immunology ; Influenza Vaccines/immunology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation/genetics ; Orthomyxoviridae Infections/immunology/prevention & control/virology ; Protein Conformation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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