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Building Polyelectrolyte Multilayers with Calmodulin: A Neutron and X-ray Reflectivity Study.

Süleyman Cinar¹, Simone Möbitz¹, Samy Al-Ayoubi¹

¹Department of Chemistry and Chemical Biology, TU Dortmund University , D-44221 Dortmund, Germany.

Langmuir : the ACS Journal of Surfaces and Colloids

|April 6, 2017

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Calmodulin (CaM) forms functional polyelectrolyte multilayers. CaM

Area of Science:

Materials Science
Biochemistry
Surface Chemistry

Background:

Calmodulin (CaM) exhibits distinct conformational states upon binding Ca2+ and ligands.
Polyelectrolyte multilayers (PEMs) are versatile thin films with tunable properties.

Purpose of the Study:

Investigate CaM's role as a polyanion in PEM formation.
Examine the impact of Ca2+ ions and trifluoperazine (TFP) on PEM structure and function.

Main Methods:

Fabrication of PEMs with CaM using a PEI-(PSS-PAH)x-CaM-PAH-CaM-PAH sequence.
Characterization of multilayer structure using X-ray and neutron reflectometry.

Main Results:

CaM deposition leads to thicker sublayers, which reduce upon PAH rinsing.

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Synthesis, Assembly, and Characterization of Monolayer Protected Gold Nanoparticle Films for Protein Monolayer Electrochemistry

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Published on: October 4, 2011

Pull-down of Calmodulin-binding Proteins

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Assembly and Characterization of Polyelectrolyte Complex Micelles

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

Trifluoperazine (TFP) does not appear to influence multilayer assembly due to CaM-PAH interactions.

PEM thickness significantly changes with Ca2+ binding to CaM, toggling between apo and holo states.

Conclusions:

CaM retains its Ca2+-dependent conformational flexibility within PEMs.
This Ca2+-induced switching offers a pathway for designing bioresponsive interfaces.