tailieunhanh - Báo cáo khoa học: Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides

There is widespread acceptance that cationic antimicrobial peptides, apart from their membrane-permeabilizing⁄disrupting properties, also operate through interactions with intracellular targets, or disruption of key cellu-lar processes. Examples of intracellular activity include inhibition of DNA and protein synthesis, inhibition of chaperone-assisted protein folding and enzymatic activity | ỊFEBS Journal MINIREVIEW Multifunctional host defense peptides intracellular-targeting antimicrobial peptides Pierre Nicolas Biogenese des Signaux Peptidiques ER3-UPMC Universite Pierre et Marie Curie Paris France Keywords antimicrobialpeptides cell-penetrating peptides dermaseptin intracellular target membrane translocation Correspondence P. Nicolas Biogenese des Signaux Peptidiques BIOSIPE ER3-UpMC Universite Pierre et Marie Curie Batiment A - 5eme etage Case courrier 29 7 Quai Saint-Bernard 75005 Paris France Fax 1 44 27 59 94 Tel 1 44 27 95 36 E-mail Received 1 May 2009 revised 25 July 2009 accepted 29 July 2009 doi There is widespread acceptance that cationic antimicrobial peptides apart from their membrane-permeabilizing disrupting properties also operate through interactions with intracellular targets or disruption of key cellular processes. Examples of intracellular activity include inhibition of DNA and protein synthesis inhibition of chaperone-assisted protein folding and enzymatic activity and inhibition of cytoplasmic membrane septum formation and cell wall synthesis. The purpose of this minireview is to question some widely held views about intracellular-targeting antimicrobial peptides. In particular I focus on the relative contributions of intracellular targeting and membrane disruption to the overall killing strategy of antimicrobial peptides as well as on mechanisms whereby some peptides are able to translocate spontaneously across the plasma membrane. Currently there are no more than three peptides that have been convincingly demonstrated to enter microbial cells without the involvement of stereospecific interactions with a receptor docking molecule and once in the cell to interfere with cellular functions. From the limited data currently available it seems unlikely that this property which is isolated in particular peptide families is also shared by the hundreds of naturally occurring .