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Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides.


ABSTRACT: Cationic antimicrobial peptides (AMPs) and host defense peptides (HDPs) show vast potential as peptide-based drugs. Great effort has been made in order to exploit their mechanisms of action, aiming to identify their targets as well as to enhance their activity and bioavailability. In this review, we will focus on both naturally occurring and designed antiviral and antitumor cationic peptides, including those here called promiscuous, in which multiple targets are associated with a single peptide structure. Emphasis will be given to their biochemical features, selectivity against extra targets, and molecular mechanisms. Peptides which possess antitumor activity against different cancer cell lines will be discussed, as well as peptides which inhibit virus replication, focusing on their applications for human health, animal health and agriculture, and their potential as new therapeutic drugs. Moreover, the current scenario for production and the use of nanotechnology as delivery tool for both classes of cationic peptides, as well as the perspectives on improving them is considered.

SUBMITTER: Mulder KC 

PROVIDER: S-EPMC3813893 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides.

Mulder Kelly C L KC   Lima Loiane A LA   Miranda Vivian J VJ   Dias Simoni C SC   Franco Octávio L OL  

Frontiers in microbiology 20131031


Cationic antimicrobial peptides (AMPs) and host defense peptides (HDPs) show vast potential as peptide-based drugs. Great effort has been made in order to exploit their mechanisms of action, aiming to identify their targets as well as to enhance their activity and bioavailability. In this review, we will focus on both naturally occurring and designed antiviral and antitumor cationic peptides, including those here called promiscuous, in which multiple targets are associated with a single peptide  ...[more]

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