Melittin exerts opposing effects on short- and long-range dynamics in bicontinuous microemulsions

V. K. Sharma, D. G. Hayes, V. S. Urban, H. O'Neill, M. Tyagi, E. Mamontov

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Bicontinuous microemulsions (BμEs) are a promising biomembrane mimetic system for investigating the behavior of antimicrobial peptides (AMPs) and their delivery to open wounds to combat antibiotic-resistant microorganisms. The properties of the BμE host are in turn affected by the guest AMP and can deviate from those of the unperturbed BμEs, especially at higher AMP concentrations. Here we report the effect of an archetypal AMP, melittin, over a wide range of concentrations, on the nanoscopic dynamics of BμEs formed by water/sodium dodecyl sulfate (SDS)/1-pentanol/dodecane, investigated using quasi-elastic neutron scattering (QENS). Two distinct motions are observed, namely, (i) the lateral motion of the surfactant on the surface of the oil channels and (ii) the internal motion of the surfactants. It is found that melittin restricts both the lateral and the internal motion, thereby acting as a stiffening agent. The lateral motion is more strongly affected, at low concentration of melittin. The lateral diffusion coefficient decreased sharply, approaching a constant value at higher melittin concentration. These results are in sharp contrast with the recent dynamic light scattering and neutron spin echo results which showed that at the length and time scales longer than those probed in the current work, melittin enhanced the long-range collective and local undulation motions of BμEs. Considered together, our results indicate that incorporation of melittin modulates the dynamics differently depending on the spatial and temporal regimes, in which the dynamics are being probed. The addition of melittin at low concentrations increased the magnitude of the zeta potential, but further increase of the melittin concentration decreased it. This suggests that addition of melittin at low concentrations led to increase in the surfactant concentration, but did not affect the negative charge per surfactant molecule, while further addition of melittin led to ion pairing of melittin with the oppositely charged surfactant. This study therefore demonstrates how the addition of melittin hinders the lateral motion of surfactants as a result of the strong association between melittin and SDS, suggesting that the release of AMPs from BμE-based delivery vehicles may be hindered.

Original languageEnglish
Pages (from-to)94-102
Number of pages9
JournalJournal of Colloid and Interface Science
Volume590
DOIs
StatePublished - May 15 2021

Funding

The research was financially supported by the Laboratory Directed Research and Development program of Oak Ridge National Laboratory. H. O'N., V.S.U. and E.M acknowledge support from ORNL's Center for Structural Molecular Biology funded by the DOE Office of Biological and Environmental Research, and from the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy. Certain commercial material suppliers are identified in this paper to foster understanding; such identification does not imply recommendation or endorsement by NIST. The research was financially supported by the Laboratory Directed Research and Development program of Oak Ridge National Laboratory. H. O'N. V.S.U. and E.M acknowledge support from ORNL's Center for Structural Molecular Biology funded by the DOE Office of Biological and Environmental Research, and from the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy. Certain commercial material suppliers are identified in this paper to foster understanding; such identification does not imply recommendation or endorsement by NIST.

FundersFunder number
Scientific User Facilities Division
U.S. Department of Energy
National Institute of Standards and Technology
Basic Energy Sciences
Biological and Environmental Research
Oak Ridge National Laboratory

    Keywords

    • Antimicrobial peptides
    • Bicontinuous microemulsions
    • Internal motions
    • Lateral motion
    • Melittin
    • Quasi-elastic neutron scattering

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