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Protein-protein Interfaces

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...

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Updated: Nov 22, 2025

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Published on: August 13, 2014

Design of biologically active binary protein 2D materials.

Ariel J Ben-Sasson^1,2, Joseph L Watson³, William Sheffler^1,2

¹Department of Biochemistry, University of Washington, Seattle, WA, USA.

|January 7, 2021

Summary

Scientists developed a computational method to create novel two-component protein arrays that self-assemble into ordered structures. These bio-inspired materials can be functionalized to control cell behavior and resist degradation, offering therapeutic potential.

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Creating Two-Dimensional Patterned Substrates for Protein and Cell Confinement

Creating Two-Dimensional Patterned Substrates for Protein and Cell Confinement

Published on: September 6, 2011

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Last Updated: Nov 22, 2025

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Published on: August 13, 2014

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

Creating Two-Dimensional Patterned Substrates for Protein and Cell Confinement

Creating Two-Dimensional Patterned Substrates for Protein and Cell Confinement

Published on: September 6, 2011

Area of Science:

Synthetic biology
Materials science
Protein engineering

Background:

Ordered two-dimensional arrays are crucial in bioengineering but typically use single protein components.
Multi-component materials offer enhanced control over assembly and functionality.
Previous designs lacked the ability to impose order on dynamic substrates like cell membranes.

Purpose of the Study:

To develop a computational method for designing co-assembling binary protein layers.
To create novel, self-assembling, multi-component protein arrays with tunable properties.
To investigate the application of these arrays in modulating cellular responses and resisting endocytosis.

Main Methods:

Computational design of rigid interfaces between dihedral protein building blocks.
In vitro self-assembly of designed protein components into p6m lattices.
Characterization using atomic force microscopy and quantitative microscopy on supported bilayers and living cells.
Functionalization of array components to create ligand-displaying surfaces.

Main Results:

Rapid, spontaneous assembly of millimolar soluble components into micrometre-scale, nearly crystalline arrays at nanomolar concentrations.
Successful design and assembly of a p6m lattice with high fidelity to computational models.
Demonstrated ability to drive receptor clustering, protein recruitment, and signaling.
Arrays imposed order on cell membranes and suppressed endocytosis, unlike antibodies or nanocages.
Tunable suppression of endocytosis offers potential for therapeutic applications.

Conclusions:

A novel computational approach enables the design of self-assembling, binary protein materials.
These materials can be precisely engineered for specific cellular interactions and functions.
The designed arrays offer a platform for synthetic cell biology, with potential therapeutic implications for modulating cell surface interactions and immune responses.