Multi-length scale structural investigation of lysozyme self-assembly

Catalini, Sara; Lutz‐Bueno, Viviane; Usuelli, Mattia; Diener, Michael; Taschin, A.; Bartolini, Paolo; Foggi, Paolo; Paolantoni, Marco; Mezzenga, Raffaele; Torre, Renato

doi:10.1016/j.isci.2022.104586

Cited by 5 publications

(3 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…6 The latter can interact with each other, forming branched structures leading to system percolation and making soft a Dipartimento di Fisica e Geologia, Universita `di Perugia, Via Pascoli, 06123 PG, matrices able to retain a large amount of solvent. [7][8][9] Among biomolecules, short peptides are attractive due to their effortless availability, programmable primary structure, and widely tunable self-assembly architecture. [10][11][12][13][14] Self-assembling of these systems depends on multiple factors, making it challenging to have a precise control over the process.…”

Section: Introductionmentioning

confidence: 99%

Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition

Catalini,

Bagni,

Cicchi

et al. 2024

Mater. Adv.

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition

Catalini,

Bagni,

Cicchi

et al. 2024

Mater. Adv.

Self Cite

View full text Add to dashboard Cite

show abstract

“…The highly concentrated environment within the compartments may also enhance the propensity of these proteins to misfold and form toxic aggregates. [ 17 ] One of the challenges barring the elucidation of the role of protein compartments in functional as well as in aberrant protein fibrillation is the complex, dynamic changes that take place within the compartment.…”

Section: Introductionmentioning

confidence: 99%

Protein Compartments Modulate Fibrillar Self‐Assembly

Karger,

Miali,

Solomonov

et al. 2023

Small

View full text Add to dashboard Cite

A notable feature of complex cellular environments is protein‐rich compartments that are formed via liquid–liquid phase separation. Recent studies have shown that these biomolecular condensates can play both promoting and inhibitory roles in fibrillar protein self‐assembly, a process that is linked to Alzheimer's, Parkinson's, Huntington's, and various prion diseases. Yet, the exact regulatory role of these condensates in protein aggregation remains unknown. By employing microfluidics to create artificial protein compartments, the self‐assembly behavior of the fibrillar protein lysozyme within them can be characterized. It is observed that the volumetric parameters of protein‐rich compartments can change the kinetics of protein self‐assembly. Depending on the change in compartment parameters, the lysozyme fibrillation process either accelerated or decelerated. Furthermore, the results confirm that the volumetric parameters govern not only the nucleation and growth phases of the fibrillar aggregates but also affect the crosstalk between the protein‐rich and protein‐poor phases. The appearance of phase‐separated compartments in the vicinity of natively folded protein complexes triggers their abrupt percolation into the compartments' core and further accelerates protein aggregation. Overall, the results of the study shed more light on the complex behavior and functions of protein‐rich phases and, importantly, on their interaction with the surrounding environment.

show abstract

“…Indeed, this globular protein, which can be easily isolated from the white of a chicken egg, has a remarkably human-like structure and can easily create amyloid aggregates in vitro. This capability is critical for understanding the molecular pathways that lead to the production of amyloid oligomers and mature amyloid fibrils [7][8][9] , which are responsible for many degenerative diseases 10 . Furthermore, lysozyme is one of the few basic proteins with a high isoelectric point, pH 11, which allows for easy charging of the protein surface by varying the pH or using other parameters such as ionic strength and protein concentration and thus shed light on the role of the excluded volume effect and the interaction potential in the formation of transient protein clusters [11][12][13] .…”

mentioning

confidence: 99%

Protein crowding effects on hydration water dynamics

Torre,

Caminiti,

Taddei

et al. 2024

Preprint

View full text Add to dashboard Cite

Water is not only a solvent in which biological molecules are dissolved, but it also plays an essential and active role in the proper development of biological processes within living organism. Water hydration shell surrounds biomolecules and has a plasticizing impact on their backbone, allowing them to execute their physiological activity in biochemical processes and biophysical modulations. Although the essential role of water in biology is evident, the comprehension of hydration water properties remains limited; the mutual influence between the protein surface and the hydration layers, on regulating structure and dynamics, remains a strongly debated question. In particular, the experimental and simulation findings on fast dynamics of hydration water are still controversial. We propose a time-resolved optical Kerr effect study of the structural and vibrational dynamics of the hydration water surrounding lysozyme on a very fast time scale. Measurements as a function of lysozyme concentration makes it possible to distinguish the hydration water contribution from that of both the bulk water and the protein. Our results provide the experimental evidence of the existence of two structural dynamics of hydration water, associated respectively with a hydrogen bond exchange relaxation process and with the reorganization of water molecules induced by protein structural fluctuations. Likewise, we evaluated the vibrational dynamics of the water hydration layer at sub-picosecond time scales. Our study of the dynamics of hydration water reveals a lysozyme clustering phenomenon prompted by the self-crowding environment, which is associated with the liquid-liquid phase separation mechanisms inherent in these protein solutions.

show abstract

Multi-length scale structural investigation of lysozyme self-assembly

Cited by 5 publications

References 57 publications

Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition

Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition

Protein Compartments Modulate Fibrillar Self‐Assembly

Protein crowding effects on hydration water dynamics

Contact Info

Product

Resources

About