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  1. European Biophysics Journal
  2. Year: 2011, Volume: 40
  3. Year: 2011, Volume: 40, Issue: 4
  4. Using zeta-potential measurements to quantify peptide partition to lipid membranes
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Year: 2016, Volume: 45
Year: 2015, Volume: 44
Year: 2014, Volume: 43
Year: 2013, Volume: 42
Year: 2012, Volume: 41
Year: 2011, Volume: 40
Year: 2011, Volume: 40, Issue: 12
Year: 2011, Volume: 40, Issue: 11
Year: 2011, Volume: 40, Issue: 10
Year: 2011, Volume: 40, Issue: 9
Year: 2011, Volume: 40, Issue: 7
Year: 2011, Volume: 40, Issue: 4
A lipocentric view of peptide-induced pores
Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering
Using zeta-potential measurements to quantify peptide partition to lipid membranes
The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action
Year: 2011, Volume: 40, Issue: 3
Year: 2011, Volume: 40, Issue: 1
Year: 2010, Volume: 39
Year: 2008, Volume: 37

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Using zeta-potential measurements to quantify peptide partition to lipid membranes

Content Provider PubMed Central
Author Freire, João M. Domingues, Marco M. Matos, Joana Melo, Manuel N. Veiga, Ana Salomé Santos, Nuno C. Castanho, Miguel A. R. B.
Abstract Many cellular phenomena occur on the biomembranes. There are plenty of molecules (natural or xenobiotics) that interact directly or partially with the cell membrane. Biomolecules, such as several peptides (e.g., antimicrobial peptides) and proteins, exert their effects at the cell membrane level. This feature makes necessary investigating their interactions with lipids to clarify their mechanisms of action and side effects necessary. The determination of molecular lipid/water partition constants (K p ) is frequently used to quantify the extension of the interaction. The determination of this parameter has been achieved by using different methodologies, such as UV-Vis absorption spectrophotometry, fluorescence spectroscopy and ζ-potential measurements. In this work, we derived and tested a mathematical model to determine the K p from ζ-potential data. The values obtained with this method were compared with those obtained by fluorescence spectroscopy, which is a regular technique used to quantify the interaction of intrinsically fluorescent peptides with selected biomembrane model systems. Two antimicrobial peptides (BP100 and pepR) were evaluated by this new method. The results obtained by this new methodology show that ζ-potential is a powerful technique to quantify peptide/lipid interactions of a wide variety of charged molecules, overcoming some of the limitations inherent to other techniques, such as the need for fluorescent labeling.
Related Links http://dx.doi.org/10.1007/s00249-010-0661-4
Ending Page 487
Page Count 7
Starting Page 481
File Format PDF
ISSN 01757571
e-ISSN 14321017
Journal European Biophysics Journal
Issue Number 4
Volume Number 40
Language English
Publisher Springer-Verlag
Publisher Date 2011-04-01
Access Restriction Open
Rights Holder Springer-Verlag
Subject Keyword Biophysics Research in Higher Education
Content Type Text
Resource Type Article
Subject Medicine Biophysics
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