Biomolecular Condensates Formed by Designer Minimalistic Peptides

27 June 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Inspired by the role of intracellular liquid-liquid phase separation (LLPS) in formation of membraneless organelles, there is great interest in developing dynamic compartments formed by LLPS of intrinsically disordered proteins (IDPs) or short peptides. However, the molecular mechanisms underlying the formation of such biomolecular condensates have not been fully elucidated, rendering on-demand design of synthetic condensates with tailored physico-chemical functionalities and responsiveness to specific stimuli a significant challenge. To address this need we have designed a library of LLPS-promoting peptide building blocks composed of various assembly domains. We show that the LLPS propensity, dynamics, and encapsulation efficiency of compartments can be tuned by specific changes to the peptide composition at the single amino acids level, with Raman and NMR spectroscopy proving instrumental in determining the molecular contribution of each side chain to droplet formation. The resulting sequence-structure-function correlation is mandatory for future development of compartments for a variety of applications.


Liquid-liquid phase separation
liquid droplets

Supplementary materials

Biomolecular Condensates Formed by Designer Minimalistic Peptides-Supplementary Information
Supplementary Information


Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.