Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The colder, the better? Sustainability in frozen storage of a monoclonal antibody drug substance.

International journal of pharmaceutics: X·2026

Same author

Dissolved oxygen effects on human growth hormone stability during freeze-thaw and metal-catalyzed oxidation.

Journal of pharmaceutical sciences·2026

Same author

New insights into the intrinsic tryptophan fluorescence emission spectra of IgG antibodies and the impact of protein unfolding and aggregation.

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V·2026

Same author

Emerging technologies and scientific advances in lyophilization of pharmaceuticals: insights from the 2025 freeze-drying of pharmaceuticals & biologicals conference.

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V·2026

Same author

Elucidating the Mechanism of Protein Particle Formation under Mechanical Stress at Different Compressible Interfaces by Molecular Dynamics and Experiments.

Molecular pharmaceutics·2026

Same author

From Bits to Bonds: High-Throughput Virtual Screening of Ribonucleic Acid Nanocarriers Using a Combinatorial Approach of Machine Learning and Molecular Dynamics.

Journal of the American Chemical Society·2025

Search research articles

Related Experiment Video

Updated: Jul 4, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Molecular Dynamics Study of Protein Aggregation at Moving Interfaces.

Tim Sarter¹, Wolfgang Friess¹

¹Department of Pharmacy, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.

Molecular Pharmaceutics

|February 7, 2024

Summary

Mechanical stress causes protein aggregation in drugs. Molecular dynamics simulations reveal how protein films at interfaces aggregate and form clusters, validating experimental findings and enabling future formulation optimization.

Keywords:

interface molecular dynamics protein aggregation protein film pumping

More Related Videos

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Related Experiment Videos

Last Updated: Jul 4, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Area of Science:

Biophysics
Computational Chemistry
Pharmaceutical Science

Background:

Protein aggregation is a major challenge in drug product stability, often triggered by mechanical stress.
Understanding protein behavior at interfaces is crucial for preventing aggregate formation.

Purpose of the Study:

To develop a molecular dynamics (MD) model for studying protein aggregation at interfaces under mechanical stress.
To quantitatively assess protein cluster formation and validate the model against experimental data.

Main Methods:

Utilized a novel MD setup with realistic human growth hormone models, including their shapes, surfaces, and interactions.
Simulated compression and dilation of protein films adsorbed to an interface.
Performed steered MD for desorption studies.

Main Results:

Simulation outcomes correlated with experimental data on subvisible particles and turbidity.
Compression speed influenced film regeneration but not aggregation behavior of preformed films.
Compressed protein systems showed increased likelihood of detaching as clusters.

Conclusions:

The developed MD model accurately reflects protein aggregation mechanisms at moving interfaces.
Compression effects at interfaces directly translate to aggregate formation in bulk solutions.
This model facilitates in silico optimization of drug formulations by studying variables like proteins, interfaces, and formulation parameters.