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Gold Binding Peptide Identified from Microfluidic Biopanning: An Experimental and Molecular Dynamics Study
Dong Jae Lee, Hyun Su Park, Kunmo Koo1
1Center for Nanomaterials and Chemical Reactions , Institute for Basic Science (IBS) , 291 Daehak-ro, Yuseong-gu , Daejeon 34141 , Republic of Korea.
Langmuir : the ACS Journal of Surfaces and Colloids
|December 29, 2018
Summary
This study introduces a microfluidic biopanning system for efficiently identifying gold-binding peptides (GBPs). The novel system precisely controls washing steps, enabling the discovery of high-affinity GBPs with potential applications in materials science.
Area of Science:
- Biotechnology
- Materials Science
- Nanotechnology
Background:
- Conventional biopanning requires extensive target materials and manual pipetting.
- Microfluidic systems offer precise control over experimental conditions, improving efficiency.
Purpose of the Study:
- To develop and validate a microfluidic biopanning system for identifying novel gold-binding peptides (GBPs).
- To analyze the binding affinity and interaction mechanisms of identified GBPs with gold surfaces.
Main Methods:
- Fabrication of a polydimethylsiloxane (PDMS) microfluidic device bonded to a gold-patterned glass slide.
- Utilizing controlled liquid flow rates and shear stress for adjustable washing steps during biopanning.
- Surface Plasmon Resonance (SPR) analysis to quantify GBP binding affinity.
- Molecular Dynamics (MD) simulations to elucidate binding interactions at the molecular level.
Main Results:
- Successful identification of a new GBP with binding affinity comparable to existing GBPs.
- Demonstrated high adjustability in the washing step of the microfluidic system.
- MD simulations revealed sequence-dependent conformations and interactions influencing GBP binding rates.
Conclusions:
- The microfluidic biopanning system is an efficient tool for discovering high-affinity peptides.
- Understanding peptide-surface interactions is crucial for designing targeted peptides.
- This approach can be adapted for identifying peptides targeting various materials.
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