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Related Experiment Video

Updated: Feb 4, 2026

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Published on: November 1, 2018

A Quantitative Model of Daptomycin Binding to Lipid Bilayers.

Antje Pokorny¹, Tala O Khatib¹, Heather Stevenson¹

¹Department of Chemistry and Biochemistry , University of North Carolina Wilmington , Wilmington , North Carolina 28403 , United States.

The Journal of Physical Chemistry. B

|September 25, 2018

Summary

Daptomycin

Area of Science:

Biochemistry
Microbiology
Pharmacology

Background:

Daptomycin is a crucial lipopeptide antibiotic for treating multidrug-resistant infections, particularly those caused by methicillin-resistant Staphylococcus aureus.
Unlike many antimicrobial peptides, daptomycin requires calcium ions (Ca2+) for binding to anionic bacterial membranes, and its efficacy is Ca2+-dependent.

Purpose of the Study:

To quantitatively model and analyze the early binding events of daptomycin to lipid bilayers.
To elucidate the precise interactions between daptomycin, lipid bilayers, and calcium ions at low drug concentrations.

Main Methods:

Utilized a quantitative model to analyze equilibrium and kinetic binding data of daptomycin to lipid bilayers.
Determined rate and equilibrium constants for daptomycin binding to lipids and Ca2+.

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Last Updated: Feb 4, 2026

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Published on: November 1, 2018

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Lipid Bilayer Vesicle Generation Using Microfluidic Jetting

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Main Results:

Developed a model involving soluble daptomycin monomers, Ca2+-bound dimers, and a 1:1 daptomycin-lipid-Ca2+ complex.
Identified a strong interaction between daptomycin and Ca2+-complexed lipids as central to its function.
Demonstrated that the availability of Ca2+ in the bulk solution influences daptomycin binding.

Conclusions:

The Ca2+-dependent binding of daptomycin to lipid bilayers is a complex process involving multiple molecular interactions.
Understanding these early binding events is critical for optimizing daptomycin's therapeutic use against resistant bacterial infections.