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Updated: Jul 15, 2025
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
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Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at
Manisha Poudyal1, Komal Patel1,2, Laxmikant Gadhe1
1Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, 400076, India.
Nature Communications
|October 4, 2023
Summary
All proteins and polypeptides can undergo liquid-liquid phase separation (LLPS), forming distinct condensates. This intrinsic property depends on electrostatic, hydrophobic, and hydrogen bonding interactions, regardless of sequence or structure.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Liquid-liquid phase separation (LLPS) is key for forming membraneless organelles.
- Intrinsically disordered regions drive protein LLPS through multivalent interactions.
Purpose of the Study:
- To investigate if LLPS is an intrinsic protein property independent of sequence and structure.
- To explore the phase regimes and driving interactions of diverse proteins and polypeptides undergoing LLPS.
Main Methods:
- Studied 23 proteins/polypeptides with varied structures and sequences.
- Assessed LLPS in the presence and absence of polyethylene glycol (PEG-8000) as a molecular crowder.
Main Results:
- All tested proteins and charged polypeptides formed liquid condensates.
- Observed distinct phase regimes and intermolecular interactions for each protein/polypeptide.
- Electrostatic, hydrophobic, and H-bonding interactions were crucial for LLPS.
Conclusions:
- LLPS is an intrinsic property of proteins and polypeptides.
- Intermolecular forces dictate the specific phase behavior of biomolecules during LLPS.
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