Protein misfolding and amyloid nucleation through liquid–liquid phase separation

Mukherjee, Semanti; Poudyal, Manisha; Dave, Kritika; Kadu, Pradeep; Maji, Samir K.

doi:10.1039/d3cs01065a

Chem. Soc. Rev.

2024

DOI: 10.1039/d3cs01065a

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Protein misfolding and amyloid nucleation through liquid–liquid phase separation

Semanti Mukherjee,

Manisha Poudyal,

Kritika Dave

et al.

Abstract: Protein misfolding and amyloid aggregation, linked to neurodegenerative diseases, can result from liquid–liquid phase separation (LLPS) and a subsequent liquid-to-solid transition. This represents LLPS as a generic mechanism in amyloid nucleation.

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Cited by 13 publications

References 479 publications

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Peptides for Liquid‐Liquid Phase Separation: An Emerging Biomaterial

Wang,

Shi

2024

ChemBioChem

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Liquid‐liquid phase separation (LLPS) refers to a spontaneous separation behavior of biomacromolecules under specific physiological conditions, playing a crucial role in regulating various biological processes. Recent advances in synthetic peptides have greatly improved our understanding of peptide‐based coacervate droplets and expanded their applications in biomedicine. Numerous peptide sequences have been reported that undergo phase separation, enabling the concentration and sequestration of different guest molecules for purposes such as drug delivery, catalytic performance, and bioanalytical techniques. Particularly, some of these peptides offer significant advantages in controlled drug release, efficient cell transfection, accelerated reaction kinetics, and selective biomarker detection. This review provides an overview of recent developments in peptide‐based LLPS, exploring various strategies for designing peptide sequences and their biomedical applications. It also addresses the challenges and future directions for LLPS peptide vehicles as promising biomaterials.

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Peptides for Liquid‐Liquid Phase Separation: An Emerging Biomaterial

Wang,

Shi

2024

ChemBioChem

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Probing Noncovalent Interactions by Fast Magic‐Angle Spinning NMR at 100 kHz and More

Schröder,

Bartalucci,

Wiegand

2024

ChemPhysChem

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Noncovalent interactions are the basis for a large number of chemical and biological molecular‐recognition processes, such as those occurring in supramolecular chemistry, catalysis, solid‐state reactions in mechanochemistry, protein folding, protein‐nucleic acid binding, and biomolecular phase separation processes. In this perspective article, some recent developments in probing noncovalent interactions by proton‐detected solid‐state Nuclear Magnetic Resonance (NMR) spectroscopy at Magic‐Angle Spinning (MAS) frequencies of 100 kHz and more are reviewed. The development of MAS rotors with decreasing outer diameters, combined with the development of superconducting magnets operating at high static magnetic‐field strengths up to 28.2 T (1200 MHz proton Larmor frequency) improves resolution and sensitivity in proton‐detected solid‐state NMR, which is the fundamental requirement for shedding light on noncovalent interactions in solids. The examples reported in this article range from protein‐nucleic acid binding in large ATP‐fueled motor proteins to a hydrogen‐π interaction in a calixarene‐lanthanide complex.

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Tailoring solid-state DNP methods to the study of α-synuclein LLPS

Jabbour,

Raran-Kurussi,

Agarwal

et al. 2024

Biophysical Chemistry

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Protein misfolding and amyloid nucleation through liquid–liquid phase separation

Abstract: Protein misfolding and amyloid aggregation, linked to neurodegenerative diseases, can result from liquid–liquid phase separation (LLPS) and a subsequent liquid-to-solid transition. This represents LLPS as a generic mechanism in amyloid nucleation.

Cited by 13 publications

References 479 publications

Peptides for Liquid‐Liquid Phase Separation: An Emerging Biomaterial

Peptides for Liquid‐Liquid Phase Separation: An Emerging Biomaterial

Probing Noncovalent Interactions by Fast Magic‐Angle Spinning NMR at 100 kHz and More

Tailoring solid-state DNP methods to the study of α-synuclein LLPS

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