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Malaria Et Peptides Antimicrobiens

Aziza Akaddar

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ISBN 10: 6131540438 / ISBN 13: 9786131540431
Published by Editions Universitaires Europeennes
New Condition: New Soft cover
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Paperback. 224 pages. Dimensions: 8.7in. x 5.9in. x 0.5in.Catestatin is an endogenous peptide derived from Chromogranin A. Bovine Catestatin and its active domain Cateslytin display powerful antimicrobial activities. We have tested the activity of bovine and human Catestatin, Cateslytin and other related peptides on in vitro growth of Plasmodium falciparum. Human Catestatin inhibits, at the micromolar range, the growth of several strains of P. falciparum. A relation structure-function analysis demonstrates the role of the LSFR median region for this activity. The non-lytic activity of Catestatin for the host cells was confirmed by its unique co-localization with merozoites. At the merozoite level we observe two complementary mechanisms: (i) a disordering (reduction in thickness) of the phosphatidylcholine component of the Plasmodium membrane by the active domain Cateslytin using solid-state NMR and polarized ATR-FTIR suggesting a penetrating peptide and (ii) a specific interaction between Catestatin and Plasmepsins II and IV leading to inhibition of haemoglobin degradation and reduction availability of nutrients for Plasmodium protein synthesis. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN. Bookseller Inventory # 9786131540431

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Bibliographic Details

Title: Malaria Et Peptides Antimicrobiens

Publisher: Editions Universitaires Europeennes

Binding: Paperback

Book Condition:New

Book Type: Paperback

About this title

Synopsis:

Catestatin is an endogenous peptide derived from Chromogranin A. Bovine Catestatin and its active domain Cateslytin display powerful antimicrobial activities. We have tested the activity of bovine and human Catestatin, Cateslytin and other related peptides on in vitro growth of Plasmodium falciparum. Human Catestatin inhibits, at the micromolar range, the growth of several strains of P. falciparum. A relation structure-function analysis demonstrates the role of the LSFR median region for this activity. The non-lytic activity of Catestatin for the host cells was confirmed by its unique co-localization with merozoites. At the merozoite level we observe two complementary mechanisms: (i) a disordering (reduction in thickness) of the phosphatidylcholine component of the Plasmodium membrane by the active domain Cateslytin using solid-state NMR and polarized ATR-FTIR suggesting a penetrating peptide and (ii) a specific interaction between Catestatin and Plasmepsins II and IV leading to inhibition of haemoglobin degradation and reduction availability of nutrients for Plasmodium protein synthesis.

About the Author:

2010 University Degree UD of Clinical InvestigatorStrasbourg University (UDS), France / 2009 Post-doctorat UDS / 2008 PhD in Microbiology UDS / 2007 UD "fighting malaria"; Faculty Pharo Marseille / 2005 Master’s Degree in Diseases’ Transmissions and humans / Pathologies, Marseille / 2003 UD of Medical Parasitology; Paris

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