Antibodies as Crypts of Antiinfective and Antitumor Peptides

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dc.contributor.authorMagliani, W.
dc.contributor.authorConti, S.
dc.contributor.authorCunha, Rodrigo Luiz Oliveira Rodrigues [UNIFESP]
dc.contributor.authorTravassos, Luiz Rodolpho [UNIFESP]
dc.contributor.authorPolonelli, L.
dc.contributor.institutionUniv Parma
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionDept Microbiol Imunol & Parasitol
dc.date.accessioned2018-06-15T17:05:13Z
dc.date.available2018-06-15T17:05:13Z
dc.date.issued2009-06-01
dc.description.abstractAntibodies (Abs), often associated with antimicrobial and antitumor agents, have emerged as an important class of novel drugs for antigen-driven therapeutic purposes in diverse clinical settings, including oncology and infectious diseases. Abs commonly give rise in the treated host to anti-Ab responses, which may induce adverse reactions and limit their therapeutic efficacy. Their modular domain architecture has been exploited to generate alternative reduced formats (Fabs, scFvs, dAbs, minibodies, multibodies), essentially devoid of the Fc region. The presence of complementarity determining regions (CDRs) ensures the maintenance of selective binding to antigens and supports their use for biotechnological and therapeutic applications. Paradigmatic Abs mimicking the wide-spectrum antimicrobial activity of a yeast killer toxin (killer Abs) have revealed the existence of a family of Abs exerting a direct in vitro and/or in vivo microbicidal activity. Based on the variable sequence of an antiidiotypic recombinant killer Ab, CDR-related peptides have been synthesized, engineered by alanine-scanning and selected according to antimicrobial, antiviral and immunomodulatory properties. Irrespective of the native Ab specificity, synthetic CDRs from unrelated murine and human monoclonal Abs, have shown to display differential in vitro, in vivo and/or ex vivo antifungal (Candida albicans), antiviral (HIV-1) and antitumor (melanoma cells) activities. Alanine substitution of single residues of synthetic CDR peptides resulted in further differential increased/unaltered/decreased biological activity. The intriguing potential of Abs as source of antiinfective and antitumor therapeutics will be discussed, in light of recent advances in peptide design, stability and delivery.en
dc.description.affiliationUniv Parma, Dipartimento Patol & Med Lab, Sez Microbiol, I-43100 Parma, Italy
dc.description.affiliationUniv Fed Sao Paulo, Dept Ciencias Exatas & Terra, Sao Paulo, Brazil
dc.description.affiliationDept Microbiol Imunol & Parasitol, Unidade Oncol Expt, Sao Paulo, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Ciencias Exatas & Terra, Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent2305-2323
dc.identifierhttp://dx.doi.org/10.2174/092986709788453104
dc.identifier.citationCurrent Medicinal Chemistry. Sharjah: Bentham Science Publ Ltd, v. 16, n. 18, p. 2305-2323, 2009.
dc.identifier.doi10.2174/092986709788453104
dc.identifier.issn0929-8673
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/43447
dc.identifier.wosWOS:000267015800005
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofCurrent Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAntibodiesen
dc.subjecttherapeutic antibodiesen
dc.subjectmicrobicidal antibodiesen
dc.subjectsynthetic CDRsen
dc.subjectkiller peptidesen
dc.subjectantiinfective peptidesen
dc.subjectantitumor peptidesen
dc.titleAntibodies as Crypts of Antiinfective and Antitumor Peptidesen
dc.typeinfo:eu-repo/semantics/article
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