Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu

Manisha Poudyal, Komal Patel, Laxmikant Gadhe, Ajay Singh Sawner, Pradeep Kadu, Debalina Datta, Semanti Mukherjee, Soumik Ray, Ambuja Navalkar, Siddhartha Maiti, Debdeep Chatterjee, Jyoti Devi, Riya Bera, Nitisha Gahlot, Jennifer Joseph, Ranjith Padinhateeri and Samir K. Maji ()
Additional contact information
Manisha Poudyal: IIT Bombay, Powai
Komal Patel: IIT Bombay, Powai
Laxmikant Gadhe: IIT Bombay, Powai
Ajay Singh Sawner: IIT Bombay, Powai
Pradeep Kadu: IIT Bombay, Powai
Debalina Datta: IIT Bombay, Powai
Semanti Mukherjee: IIT Bombay, Powai
Soumik Ray: IIT Bombay, Powai
Ambuja Navalkar: IIT Bombay, Powai
Siddhartha Maiti: IIT Bombay, Powai
Debdeep Chatterjee: IIT Bombay, Powai
Jyoti Devi: IIT Bombay, Powai
Riya Bera: IIT Bombay, Powai
Nitisha Gahlot: IIT Bombay, Powai
Jennifer Joseph: IIT Bombay, Powai
Ranjith Padinhateeri: IIT Bombay, Powai
Samir K. Maji: IIT Bombay, Powai

Nature Communications, 2023, vol. 14, issue 1, 1-21

Abstract: Abstract Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon underlying the sequestration of macromolecules (such as proteins and nucleic acids) into membraneless organelles in cells. Unstructured and intrinsically disordered domains are known to facilitate multivalent interactions driving protein LLPS. We hypothesized that LLPS could be an intrinsic property of proteins/polypeptides but with distinct phase regimes irrespective of their sequence and structure. To examine this, we studied many (a total of 23) proteins/polypeptides with different structures and sequences for LLPS study in the presence and absence of molecular crowder, polyethylene glycol (PEG-8000). We showed that all proteins and even highly charged polypeptides (under study) can undergo liquid condensate formation, however with different phase regimes and intermolecular interactions. We further demonstrated that electrostatic, hydrophobic, and H-bonding or a combination of such intermolecular interactions plays a crucial role in individual protein/peptide LLPS.

Date: 2023
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DOI: 10.1038/s41467-023-41864-9

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