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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Published on: April 23, 2017

Affinity-based Protein Surface Pattern Formation by Ligand Self-Selection from Mixed Protein Solutions.

David W Grainger1, David G Castner, Manish Dubey

  • 1Departments of Pharmaceutics and Pharmaceutical Chemistry, and Bioengineering, University of Utah, Salt Lake City, UT 84112-5820 (USA).

Advanced Functional Materials
|March 19, 2013
PubMed
Summary

This study demonstrates a novel method for creating precise protein patterns on surfaces using self-selection. This technique ensures high specificity and fidelity for applications in biosensing and diagnostics.

Keywords:
ToF-SIMSpatterned proteinsphotolithographypoly(ethylene glycol)protein imaging

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Protein Engineering by Yeast Surface Display
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Protein Engineering by Yeast Surface Display

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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Area of Science:

  • Surface chemistry
  • Biotechnology
  • Materials science

Background:

  • Precise patterning of proteins on surfaces is crucial for developing advanced biosensors and diagnostic tools.
  • Existing methods often face challenges with specificity and non-specific adsorption.
  • Developing robust and high-fidelity protein patterning techniques is an ongoing area of research.

Purpose of the Study:

  • To develop a method for creating high-fidelity, specific surface patterns of two distinct proteins from a mixed solution.
  • To investigate the effectiveness of photolithographically patterned affinity ligands for protein self-selection.
  • To evaluate the specificity and fidelity of protein patterning using fluorescence imaging and Time-of-Flight Secondary Ion Mass Spectrometry (ToF-SIMS).

Main Methods:

  • Photolithography was used to create surface patterns of biotin and chloroalkane ligands.
  • Mixed solutions of streptavidin and HaloTag® proteins were used for spontaneous surface patterning.
  • Protein immobilization was assessed using fluorescence imaging.
  • Chemical specificity and non-specific adsorption were analyzed using ToF-SIMS imaging.
  • Principal Component Analysis (PCA) was applied to ToF-SIMS data for enhanced pattern discrimination.

Main Results:

  • High-fidelity surface patterns of streptavidin and HaloTag® were successfully formed via self-selection onto their respective ligands.
  • Fluorescence imaging confirmed high specificity of protein binding to patterned ligands.
  • ToF-SIMS imaging validated the chemical specificity of protein-ligand interactions.
  • Non-specific adsorption of bovine serum albumin was detected, indicating a limitation for masking proteins.
  • PCA of ToF-SIMS data improved the discrimination between different patterned proteins.

Conclusions:

  • Spontaneous protein self-selection onto patterned affinity ligands offers a robust method for creating high-fidelity protein surfaces.
  • The combination of fluorescence imaging and ToF-SIMS with PCA provides powerful tools for characterizing patterned protein surfaces.
  • Further optimization is needed to minimize non-specific adsorption of excess proteins in complex solutions.