We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience. You can read our Cookie Policy here.

Advertisement

Noncovalent Polymerization of Mesogens Crystallizes Lysozyme: Correlation Between Nonamphiphilic Lyotropic Liquid Crystal Phase and Protein Crystal Formation


Want a FREE PDF version of This News Story?

Complete the form below and we will email you a PDF version of "Noncovalent Polymerization of Mesogens Crystallizes Lysozyme: Correlation Between Nonamphiphilic Lyotropic Liquid Crystal Phase and Protein Crystal Formation"

Technology Networks Ltd. needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy

Read time:
 

Abstract
Crystallization of proteins is important for fundamental studies and biopharmaceutical development but remains largely an empirical science. Certain nonamphiphilic organic molecules with fused aromatic rings and two charges can assemble into stable thread-like noncovalent polymers that may further form liquid crystal phases in water, traditionally termed chromonic liquid crystals. Using five of these mesogenic molecules as additives to induce protein crystallization, we discover that molecules that can form liquid crystal phases in water are highly effective at inducing the crystal formation of lysozyme, even at concentrations significantly lower than that required for forming liquid crystal phases. This result reveals an example of inducing protein crystallization by the molecular assembly of the additives, and is consistent with a new mechanism by which the strong hydration of an assembly process provides a gradual means to compete for the water molecules to enable solvated proteins to form crystals.

The Author Manuscript is published online in Langmuir and is free to access.

Advertisement