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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: Dec 16, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Engineering Biomolecular Self-Assembly at Solid-Liquid Interfaces.

Shuai Zhang^1,2, Jiajun Chen^1,2, Jianli Liu^2,3

¹Department of Materials Science and Engineering, University of Washington, Seattle, WA, 98105, USA.

Advanced Materials (Deerfield Beach, Fla.)

|July 7, 2020

Summary

This summary is machine-generated.

Researchers are advancing biomolecular self-assembly at interfaces for novel biomaterials. This work summarizes progress in programming peptides, proteins, and peptoids for bottom-up material design.

Keywords:

biomolecular self-assembly peptides peptoids proteins solid-liquid interfaces

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Area of Science:

Biomolecular engineering
Bionanotechnology
Materials science

Background:

Life utilizes biomolecular self-assembly for bottom-up construction of functional materials.
Bioengineering and bionanotechnology have adopted this strategy for designing diverse biomolecular and hybrid materials.
Controlling self-assembly at solid-liquid interfaces lags behind bulk solution methods.

Purpose of the Study:

To summarize recent achievements in programming biomolecular self-assembly at solid-liquid interfaces.
To describe applications of engineered biomolecular self-assembly at interfaces.
To discuss advances in understanding self-assembly pathways at interfaces.

Main Methods:

Review of recent literature on programming self-assembly of peptides, proteins, and peptoids.
Analysis of applications in biomaterials design.
Discussion of in situ atomic force microscopy studies for physical understanding.

Main Results:

Progress has been made in programming self-assembly of peptides, proteins, and peptoids at solid-liquid interfaces.
Various applications of interface-driven biomolecular self-assembly are emerging.
In situ atomic force microscopy provides new physical insights into self-assembly pathways.

Conclusions:

Advances in programming biomolecular self-assembly at interfaces are enabling new biomaterial design strategies.
Improved understanding of interfacial self-assembly pathways is crucial for future innovations.
This field holds promise for creating novel biomaterials interfaced with inorganic surfaces.