Entropic (de)stabilization of surface-bound peptides conjugated with polymers

Area of Science:

• Biotechnology
• Polymer Science
• Biophysics

Background:

• Functional proteins must maintain native structures at interfaces for biotechnologies.
• Surface interactions significantly impact protein thermostability, necessitating stabilization strategies.

Purpose of the Study:

• To investigate how polymer conjugation affects the secondary structure and thermostability of surface-tethered peptides.
• To develop a predictive model for polymer-induced stabilization of surface-bound proteins.

Main Methods:

• Utilized molecular dynamics simulations of coarse-grained helical peptides conjugated to polymers.
• Varied polymer lengths and conjugation sites to observe effects on peptide folding.
• Applied ideal-chain polymer entropies to explain and predict thermostability shifts.

Main Results:

• Polymer conjugation demonstrated significant control over peptide secondary structure and thermostability.
• Observed diverse stabilizing and destabilizing effects based on polymer variations.
• Ideal-chain polymer entropies accurately predicted shifts in folding temperature.

Conclusions:

• Polymer conjugation offers a tunable method to control protein folding and thermostability at interfaces.
• A theoretical model based on ideal-chain entropies can predict critical polymer lengths for protein stabilization.
• Findings provide design strategies for stabilizing surface-associated proteins in various technological applications.