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Published on: February 27, 2019
Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides
Urartu Ozgur Safak Seker1, Brandon Wilson, Sevil Dincer
1Genetically Engineered Materials Science and Engineering Center, Materials Science and Engineering, University of Washington, Seattle, WA 98195, USA.
Constraining peptide structure with Cys-Cys loops enhances platinum binding affinity and kinetics. This finding offers insights into designing inorganic-binding peptides for bionanotechnology applications.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Peptide Engineering
Background:
- Phage and cell-surface display libraries enable selection of peptides that bind inorganic materials.
- Understanding the molecular mechanisms of peptide-inorganic interactions is crucial for their application.
- Current knowledge of binding kinetics and thermodynamics for inorganic-binding peptides is limited.
Purpose of the Study:
- To investigate the impact of structural constraints on the binding characteristics of inorganic-binding peptides.
- To compare the adsorption behavior and conformational properties of a cyclic versus a linear platinum-binding peptide.
- To explore how structural modifications can tune peptide adsorption and binding features for bionanotechnological applications.
Main Methods:
- Synthesized a cyclic (Cys-Cys constrained) and a linear platinum-binding peptide sequence.
- Analyzed peptide adsorption on platinum thin films using surface plasmon resonance (SPR) spectroscopy.
- Determined peptide conformational properties using circular dichroism (CD) spectroscopy and 2,2,2-trifluoroethanol (TFE) titrations.
Main Results:
- The cyclic peptide exhibited significantly higher equilibrium and adsorption rate constants, indicating stronger and faster binding, with 1:1 Langmuir adsorption.
- The linear peptide displayed slower and weaker binding with biexponential Langmuir isotherm behavior.
- Conformational analysis revealed the cyclic peptide adopted a random coil, while the linear peptide adopted a polyproline type II conformation in equilibrium with a random coil.
Conclusions:
- Cys-Cys constraints significantly alter the conformation and binding behavior of platinum-binding peptides.
- Structural constraints can be strategically employed to modulate the adsorption properties of inorganic-binding peptides.
- This study provides a foundation for genetically designing peptides with tailored binding affinities and kinetics for bionanotechnology.
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