Charged Surface Regulates the Molecular Interactions of Electrostatically Repulsive Peptides by Inducing Oriented...

Area of Science:

• Computational chemistry
• Biophysics
• Surface science

Background:

• Charged protein aggregation is a significant challenge in biotechnology.
• Understanding molecular interactions at charged surfaces is crucial for controlling protein behavior.

Purpose of the Study:

• To investigate how like-charged surfaces regulate the orientation and interactions of charged peptides.
• To provide molecular-level insights into the mechanisms of electrostatic repulsion between peptides.

Main Methods:

• All-atom molecular dynamics simulations were employed.
• Analysis focused on molecular orientation, electrostatic interactions, and peptide alignment.

Main Results:

• Like-charged surfaces induce oriented alignment of charged peptides.
• This alignment enhances electrostatic repulsion between peptide molecules.
• Peptides with electric dipole structures showed distinct regulation effects.

Conclusions:

• Charged surfaces and peptide dipole structure are key to regulating peptide interactions.
• Findings support experimental observations on inhibiting protein aggregation.
• This research can guide the design of surfaces for controlling amphoteric molecule behavior in vivo and in vitro.