Prof. Octavio L. Franco, Universidade Católica de Brasília, Brazil
Biograph: Graduate at Ciências Biológicas from Universidade Federal do Ceará (1998) and PHd at Biochemistry and Molecular Biology from Universidade de Brasília (2001). Actually is head professor from Universidade Catolica Dom Bosco and Universidade Catolica de Brasilia, and researcher from CNPq. At the moment is consultor of CNPq, FAPEMIG, FINEP, FAPDF, FUNDCET, FAPEMA, FUNDECT, FUNCAP, CPP, FONCYT, CONICYT, FAPESB, FACEPE, Kazakistan government, BARD United States - Israel Binational Agricultural Research and Development Fund, Austrian Science Fundation, Gates Foundation e National Science Foundation (NSF) US .Member of Sociedade Brasileira de Bioquimica e Biologia Molecular (SBBq), The American Society for Biochemistry and Molecular Biology (ASBMB) and American Association for the Advancement of Science (AAAS). Has experience in Biochemistry, proteomics and molecular modeling. Acting on the following subjects: antimicrobial peptides, immunomodulators, antifreezing and proteome of animals, plants and microorganisms. Also have his work focused on the development of bioproducts and bioprocesses. Published almost 300 articles in different international journals. Moreover, is also editor of Scientific Reports, Frontiers in Microbiology and participate as a board member of dozens of journals.

Speech Title: In silico optimization of antimicrobial peptide enables combinatorial exploration for peptide design
Abstract: Several organisms including plants and sea animals are extensively used in traditional medicine and are excellent sources of natural products. Several antimicrobial peptides (AMPs) from naural sources have been described and proposed as alternatives to conventional antibiotics. Here, we describe the use of a genetic algorithm to design synthetic AMPs derived from plant (Pg-AMP1) a glycine-rich peptide previously isolated from guava seeds and sea animal (clavanins). This approach yielded both peptides classes that possess an unusually high proportion of arginines and use tyrosine residues as hydrophobic counterparts. Guavanin 2 emerged as a prototype AMP, among fifteen guavanin analogues screened for their activity against an engineered luminescent strain of Pseudomonas aeruginosa. Similarly, clavanin-MO was also selected. Both peptides were further characterized in terms of structure, activity and biotechnological potential. These novel peptides were unstructured in water and underwent a coil-to helix transition in hydrophobic environments. This conformation was corroborated by NMR analysis in dodecylphosphocholine micelles, which revealed an α-helical structure. Guavanin 2 and clavanin-MO caused a bactericidal effect at low micromolar concentrations, causing membrane disruption, without triggering depolarization but rather hyperpolarization. The present work presents a computational approach to explore natural products for the design of short and potent peptide antibiotics.