Proline isomerization regulates the phase behavior of elastin-like polypeptides in water

TL;DR

This study investigates how proline isomerization affects the phase behavior of elastin-like polypeptides in water, revealing that cis isomers significantly influence their collapse and interactions, which is crucial for biomedical and material applications.

Contribution

It provides new insights into how cis/trans proline isomerization modulates ELP phase behavior, advancing understanding of IDP responsiveness in aqueous environments.

Findings

Cis proline isomers hinder peptide-water hydrogen bonding.

Cis isomers promote intramolecular interactions.

Proline isomerization tunes the LCST transition of ELPs.

Abstract

Responsiveness of polypeptides and polymers in aqueous solution plays an important role in biomedical applications and in designing advanced functional materials. Elastin-like polypeptides (ELPs) are a well-known class of synthetic intrinsically disordered proteins (IDPs), which exhibit a lower critical solution temperature (LCST) in pure water. The LCST transition can be further tuned by proline isomerization. Here, we study and compare the influence of cis/trans proline isomerization on the collapse of single ELPs in aqueous solution. Our results reveal that cis isomers play an important role in tuning the phase behavior of ELPs by hindering peptide-water hydrogen bonding while promoting intramolecular interactions.