NDLI: Elucidating the mechanism of peptide interaction with membranes using the intrinsic fluorescence of tryptophan: perpendicular penetration of cecropin B-like peptides into Pseudomonas aeruginosa

Content Provider	Royal Society of Chemistry (RSC)
Author	Abou-Zied, Osama K. Barbour, Abdelahhad Philip, Koshy Al-Sharji, Nada A.
Copyright Year	2015
Abstract	The importance of small molecular weight antimicrobial peptides as novel therapeutic agents stems from their ability to act against bacteria, viruses, and fungi. As part of the innate immune system, they are also capable of killing cancerous cells. Herein, we study the interaction between a synthetic cecropin B peptide and a target Pseudomonas aeruginosa (PA) membrane using steady-state and time-resolved fluorescence measurements in order to elucidate the mechanism of membrane rupture. The importance of synthetic cecropin B as a therapeutic peptide stems from its effect against a wide range of bacteria which is indistinguishable from that of naturally occuring cecropins. Fluorescence of cecropin B results from the sole tryptophan residue in the peptide. In order to understand the mechansim of peptide–membrane binding, we modified the original peptide (cecropin B1: KWKVFKKIEKMGRNIRNGIV) by attaching a terminal tryptophan residue (cecropin B2: KWKVFKKIEKMGRNIRNGIVW). Both peptides show a large inhibition effect against a wide range of bacteria, compared to naturally occurring peptides. The fluorescence results show an enhancement in the peak intensity of cecropin B1 upon mixing with the membrane, accompanied by a blue shift. For cecropin B2, a blue shift was observed upon mixing with the PA membrane, but no enhancement in intensity was observed. The results indicate perpendicular penetration of cecropins B1 and B2 from the Lys side where the Trp residue of cecropin B1 is immersed in the PA membrane. Partial quenching of the Trp fluorescence by acrylamide was observed and the values of the Stern–Volmer constants (Ksv) indicate that the Trp molecule penetrates into the membrane, but resides close to the interface region. Two fluorescence lifetimes were measured for the cecropin B1–PA complex which are for two rotamers of Trp. The results point to a degree of flexibility of the local environment around the Trp molecule. A mechanism of membrane disruption is proposed in which the cecropin peptide creates cracks through the negatively charged outer membrane of PA.
Starting Page	14214
Ending Page	14220
Page Count	7
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	5
Issue Number	19
Journal	RSC Advances
DOI	10.1039/c4ra15246h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Volmer Fluorescence Tryptophan Innate immune system Pseudomonas Fungus Acrylamide Trp Blueshift Lysine Antimicrobial peptides Bacteria Cecropin Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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