Saccone, Irene (2016) Design and Synthesis of Peptide and Peptidomimetics Involved in Antiretroviral and Anticancer Therapies. [Tesi di dottorato]
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Item Type: | Tesi di dottorato |
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Resource language: | English |
Title: | Design and Synthesis of Peptide and Peptidomimetics Involved in Antiretroviral and Anticancer Therapies |
Creators: | Creators Email Saccone, Irene irene.saccone@unina.it |
Date: | 23 March 2016 |
Number of Pages: | 133 |
Institution: | Università degli Studi di Napoli Federico II |
Department: | Farmacia |
Scuola di dottorato: | Scienze farmaceutiche |
Dottorato: | Scienza del farmaco |
Ciclo di dottorato: | 28 |
Coordinatore del Corso di dottorato: | nome email D'Auria, Valeria EMAIL mariavaleria.dauria@unina.i |
Tutor: | nome email Santagada, Vincenzo UNSPECIFIED |
Date: | 23 March 2016 |
Number of Pages: | 133 |
Keywords: | NC inhibitors, 2,6-dipeptidilantraquinones, IGFBP6 fragment, auxiliary |
Settori scientifico-disciplinari del MIUR: | Area 03 - Scienze chimiche > CHIM/08 - Chimica farmaceutica |
Date Deposited: | 11 Apr 2016 07:43 |
Last Modified: | 11 May 2017 01:00 |
URI: | http://www.fedoa.unina.it/id/eprint/10706 |
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Abstract Unit 1 The development of new anti-HIV-1 drugs is a global need, due to the resistance and the side effects arising from the therapies currently in use, for this reason we focused on an innovative target, the nucleocapsidic chaperonic protein(NC) of HIV-1 virus, which is involved in many steps of the virus replication, expecially the trascription. Moreover it plays a role of mediator in the annealing reaction of TAR with cTAR. 2,6-Dipeptidyl-anthraquinones are a promising class of nucleic acid-binding compounds that act as NC inhibitors in vitro. We designed, synthesized and tested new series of 2,6-disubstituted-anthraquinones, which are able to bind viral nucleic acid substrates of NC. We demonstrated that these novel derivatives interact preferentially with non-canonical structures of TAR and cTAR, stabilize their dynamics structures, such as bulge and loop, and interfere with NC chaperone activity.
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