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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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Related Experiment Video

Updated: Jul 22, 2025

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Nanobio Interface Between Proteins and 2D Nanomaterials.

Shounak Roy^1,2, Aastha¹, Kaivalya A Deo²

¹School of Biosciences and Bioengineering, Indian Institute of Technology, Mandi, Kamand, Mandi, Himachal Pradesh 175075, India.

ACS Applied Materials & Interfaces

|July 24, 2023

Summary

This summary is machine-generated.

Understanding protein interactions with two-dimensional (2D) nanomaterials is crucial for their safe biomedical use. This review explores these interactions and analytical methods to guide the design of 2D nanomaterials for theranostics.

Keywords:

2D nanomaterial analytical tools interaction forces protein corona surface energy

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Last Updated: Jul 22, 2025

Monitoring Protein Adsorption with Solid-state Nanopores

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Published on: December 2, 2011

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Area of Science:

Material Science
Nanotechnology
Biomedical Engineering

Background:

Two-dimensional (2D) nanomaterials offer unique properties for advanced applications.
Their biomedical translation is hindered by limited understanding of interactions within biological systems.
Protein interactions significantly influence nanomaterial behavior and biological identity.

Purpose of the Study:

To review protein-2D nanomaterial interactions in biological microenvironments.
To discuss analytical techniques for characterizing these interactions.
To guide the safer design of 2D nanomaterials for theranostic applications.

Main Methods:

Literature review of protein-nanomaterial interactions.
Analysis of how biological moieties affect nanomaterial properties.
Survey of analytical techniques for studying these interfaces.

Main Results:

Protein adsorption alters nanomaterial size, charge, shape, and composition.
These alterations critically impact nanomaterial biological activity.
Various analytical methods exist to study these complex interactions.

Conclusions:

A comprehensive understanding of protein-2D nanomaterial interplay is essential.
This knowledge is key to mitigating risks and optimizing 2D nanomaterials for biomedical applications.
Safer design strategies can leverage this understanding for advanced theranostics.