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  • Title: Interaction of self-assembling beta-sheet peptides with phospholipid monolayers: the role of aggregation state, polarity, charge and applied field.
    Author: Protopapa E, Maude S, Aggeli A, Nelson A.
    Journal: Langmuir; 2009 Mar 03; 25(5):3289-96. PubMed ID: 19437790.
    Abstract:
    Studies of beta-sheet peptide/phospholipid interactions are important for an understanding of the folding of beta-sheet-rich membrane proteins and the action of antimicrobial and toxic peptides. Further, self-assembling peptides have numerous applications in medicine and therefore an insight is required into the relation between peptide molecular structure and biomembrane activity. We previously developed one of the simplest known model peptide systems which, above a critical concentration (c*) in solution, undergoes nucleated one-dimensional self-assembly from a monomeric random coil into a hierarchy of well defined beta-sheet structures. Here we examine the effects of peptide aggregation, polarity, charge, and applied field on peptide interactions with dioleoyl phosphatidylcholine (DOPC) monolayers using electrochemical techniques. The interactions of six systematically altered 11 residue beta-sheet tape-forming peptides were investigated. The following findings with respect to 11 residue beta-sheet peptide-DOPC interaction arose from the study: (i) The solution monomer peptide species is the monolayer active moeity. (ii) Amphiphilic peptides are more monolayer active than polar peptides in the absence of applied electric field. (iii) Positive charge on amphiphilic peptides facilitates monolayer interaction in the absence of applied electric field. (iv) Negative applied electric field facilitates monolayer interaction with positively charged amphiphilic and polar peptides. (v) Neutral amphiphilic peptides permeabilize DOPC layers to ions to the greatest extent. (vi) The beta-sheet tape forming peptides are shown to be significantly less monolayer disruptive than antimicrobial peptides. These conclusions will greatly contribute to the rational design of new peptide-based biomaterials and biosensors.
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