TAILIEUCHUNG - Báo cáo khoa học: Structural aspects and biological properties of the cathelicidin PMAP-36

PMAP-36 is a cathelicidin-derived host defence peptide originally deduced by a transcript from pig bone marrow RNA. The expression of the propep-tide in leukocytes, and the structure, antimicrobial activity, and mechanism of action of the mature peptide were investigated. The proform is stored as a dimeric precursor of 38 kDa formed by a dimerization site at its C-ter-minal cysteine residue; it is likely that the mature peptide is dimeric when released. | iFEBS Journal Structural aspects and biological properties of the cathelicidin PMAP-36 Marco Scocchi Igor Zelezetsky Monica Benincasa Renato Gennaro Andrea Mazzoli and Alessandro Tossi Department of Biochemistry Biophysics and Macromolecular Chemistry University of Trieste Italy Keywords antimicrobialpeptide cathelicidin homodimer membrane permeabilization PMAP-36 Correspondence M. Scocchi Department of Biochemistry Biophysics and Macromolecular Chemistry University of Trieste 34127 Trieste Italy Fax 39 040558 3691 Tel 39 040558 3990 E-mail scocchi@ Received 29 April2005 revised 24 June 2005 accepted 7 July 2005 doi PMAP-36 is a cathelicidin-derived host defence peptide originally deduced by a transcript from pig bone marrow RNA. The expression of the propeptide in leukocytes and the structure antimicrobial activity and mechanism of action of the mature peptide were investigated. The proform is stored as a dimeric precursor of 38 kDa formed by a dimerization site at its C-ter-minal cysteine residue it is likely that the mature peptide is dimeric when released. Monomeric and dimeric forms of PMAP-36 were chemically synthesized and their activity compared. Both forms assumed an amphipathic a-helical conformation and exhibited a potent and rapid microbicidal activity against a wide spectrum of microorganisms mediated by their ability to permeabilize the microbial membranes rapidly. A shortened fragment localized the helical region to the N terminus but showed a significantly lower potency and slower permeabilization kinetics indicating an important role of the nonhelical C-terminal hydrophobic portion of this molecule. Dimerization modulated the effectiveness of the peptide in terms of killing and permeabilization kinetics and reduced medium dependence. It allows the molecule to achieve an impressive charge density 28 in 70 residues although the significance of this feature with respect to biological activity has yet to be

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