Ubiquicidin-Derived Peptides Selectively Interact with the Anionic Phospholipid Membrane
Jyotsna Bhatt Mitra1, Veerendra K Sharma1, Archana Mukherjee1
1Homi Bhabha National Institute , Anushaktinagar , Mumbai 400094 , India.
Langmuir : the ACS Journal of Surfaces and Colloids
|December 4, 2019
Summary
Ubiquicidin-derived peptides interact with anionic membranes, impacting vesicle aggregation and lipid dynamics. UBI (29-41) restricts lipid motion more than UBI (31-38), informing antimicrobial peptide probe design.
Area of Science:
- Biophysics
- Membrane Biophysics
- Antimicrobial Peptides
Background:
- Ubiquicidin (UBI)/ribosomal protein S30 (RS30) exhibits antimicrobial properties.
- UBI-derived peptides, UBI (29-41) and UBI (31-38), show promise as infection imaging probes.
Purpose of the Study:
- To investigate the interaction mechanism of UBI-derived peptides with anionic and zwitterionic phospholipid membranes.
- To elucidate the effects of these peptides on model bacterial membrane dynamics.
Main Methods:
- Isothermal titration calorimetry (ITC) to study binding thermodynamics.
- Dynamic light scattering (DLS) to assess vesicle aggregation.
- Quasielastic neutron scattering (QENS) to probe microscopic lipid dynamics.
Main Results:
- Both UBI peptides selectively bind to anionic membranes, driven by exothermic enthalpy and entropy.
- Peptide binding induces anionic vesicle aggregation, more pronounced with UBI (29-41).
- QENS reveals peptides restrict lipid lateral motion, with UBI (29-41) being a stronger stiffening agent.
Conclusions:
- This study provides the first mechanistic insight into UBI-derived peptide interactions with model membranes.
- Findings are crucial for designing improved antimicrobial peptide-based infection imaging agents.
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