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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Balhara, Vinod Schmidt, Rolf Dewolf, Christine Gorr, Sven-ulrik |
| Description | Author Affiliation: Balhara V ( Department of Chemistry and Biochemistry and the Centre for NanoScience Research, Concordia University, 7141 Sherbrooke St. W., Montreal, Quebec H4B 1R6, Canada.) |
| Abstract | GL13K is a short (13 amino acid) antimicrobial peptide derived from the parotid secretory protein. GL13K has been found to exhibit anti-inflammatory and antibacterial activities in physiological salt conditions. We investigated the mechanism of interaction of GL13K, with model membranes comprising 1, 2-dioleoylphosphatidylcholine (DOPC) and 1, 2-dioleoylphosphatidylglycerol (DOPG) using various biophysical and imaging techniques. Circular dichroism studies showed that GL13K adopts a β-sheet structure in the presence of negatively charged DOPG liposomes while it retains its random coil structure with zwitterionic DOPC liposomes. GL13K did not cause any fusion of these liposomes but was able to selectively disrupt the negatively charged membranes of DOPG leading to vesicular leakage. There was no or minimal evidence of GL13K interaction with DOPC liposomes, however an analysis of supported lipid bilayers (SLBs) using atomic force microscopic (AFM) imaging and dual polarization interferometry (DPI) suggested that GL13K can interact with the surface of a DOPC planar bilayer. In the case of DOPG bilayers, AFM and DPI clearly showed membrane thinned regions where a portion of lipid molecules has been removed. These results suggest that the mechanism of GL13K action on bacterial membranes involves localized removal of lipid from the membrane via peptide-induced micellization. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1828 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Antimicrobial Cationic Peptides Chemistry Lipid Bilayers Liposomes Phosphatidylcholines Phosphatidylglycerols Circular Dichroism Microscopy, Atomic Force Protein Structure, Secondary Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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