How binding to surfaces affects disorder?

Bartolo, Ary Lautaro Di; Masone, Diego

doi:10.1016/b978-0-323-99533-7.00017-0

Cited by 3 publications

(4 citation statements)

References 273 publications

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“…The organization of the lipid bilayer responds to the most favorable energy state, with hydrophilic heads in contact with water and hydrophobic tails buried between other lipids. , Although a reduced resolution model, MARTINI has demonstrated over the last two decades that its parametrization correctly captures most of the basic characteristics of many biological systems. − …”

Section: Resultsmentioning

confidence: 99%

“…Intrinsically disordered regions in proteins that bind to the lipid bilayer add substantial complexity to the molecular description of the lipid–protein interplay in biological events, such as the nucleation of the fusion pore and its further expansion. , As pointed out by Uversky et al more than 20 years ago for α-synuclein, its extraordinary how a protein with an unstructured region is transformed into highly organized fibrils. Therefore, significant efforts have been made to improve computational modeling of intrinsically disordered proteins. − …”

Section: Introductionmentioning

confidence: 99%

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Intrinsic Disorder in α-Synuclein Regulates the Exocytotic Fusion Pore Transition

Bartolo

Caparotta

Masone

2023

ACS Chem. Neurosci.

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Today, it is widely accepted that intrinsic disorder is strongly related to the cell cycle, during mitosis, differentiation, and apoptosis. Of particular interest are hybrid proteins possessing both structured and unstructured domains that are critical in human health and disease, such as α-synuclein. In this work, we describe how α-synuclein interacts with the nascent fusion pore as it evolves toward expansion. We unveil the key role played by its intrinsically disordered region as a thermodynamic regulator of the nucleation-expansion energy barrier. By analyzing a truncated variant of α-synuclein that lacks the disordered region, we find that the landscape of protein interactions with PIP2 and POPS lipids is highly altered, ultimately increasing the energy cost for the fusion pore to transit from nucleation to expansion. We conclude that the intrinsically disordered region in full-length α-synuclein recognizes and allocates pivotal protein:lipid interactions during membrane remodeling in the first stages of the fusion pore.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Intrinsic Disorder in α-Synuclein Regulates the Exocytotic Fusion Pore Transition

Bartolo

Caparotta

Masone

2023

ACS Chem. Neurosci.

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“…An update on how disorder in turn is affected during interaction with biological surfaces in general is available (Di Bartolo & Masone, 2023). Lately, there has been a vigorous renewal of interest in understanding protein interactions with surfaces of nanoparticles which has, again, importance in both in vivo and in vitro (Gupta & Roy, 2020; Mukherjee & Gupta, 2016a; Sousa et al, 2021).…”

Section: Interactions Of Idps/idrs With Other Proteins and Surfaces I...mentioning

confidence: 99%

Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure

Gupta,

Uversky

2024

Protein Science

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The rationale for replacing the old binary of structure–function with the trinity of structure, disorder, and function has gained considerable ground in recent years. A continuum model based on the expanded form of the existing paradigm can now subsume importance of both conformational flexibility and intrinsic disorder in protein function. The disorder is actually critical for understanding the protein–protein interactions in many regulatory processes, formation of membrane‐less organelles, and our revised notions of specificity as amply illustrated by moonlighting proteins. While its importance in formation of amyloids and function of prions is often discussed, the roles of intrinsic disorder in infectious diseases and protein function under extreme conditions are also becoming clear. This review is an attempt to discuss how our current understanding of protein function, specificity, and evolution fit better with the continuum model. This integration of structure and disorder under a single model may bring greater clarity in our continuing quest for understanding proteins and molecular mechanisms of their functionality.

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“…Phase differences are caused by the lower speed of light in aqueous media compared to air and can be visualized by methods such as phase contrast or differential interference contrast (DIC) microscopy. Remarkably, label-free quantitative DIC has revealed phase transitions in lipid bilayers down to 0.1-nm precision [ 23 ]. Transitions between liquid-ordered and liquid-disordered lipid phases are increasingly important in virus infections both for entry, replication and egress [ 24–26 ].…”

Section: Transmitted Light Microscopymentioning

confidence: 99%

Label-free microscopy for virus infections

2023

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Microscopy has been essential to elucidate micro- and nano-scale processes in space and time, and has provided insight into cell and organismic function. It is widely employed in cell biology, microbiology, physiology, clinical sciences and virology. While label-dependent microscopy, such as fluorescence microscopy, provides molecular specificity, it has remained difficult to multiplex in live samples. In contrast, label-free microscopy reports on overall features of the specimen at minimal perturbation. Here, we discuss modalities of label-free imaging at the molecular, cellular and tissue levels, including transmitted light microscopy, quantitative phase imaging, cryogenic electron microscopy or tomography, and atomic force microscopy. We highlight how label-free microscopy is used to probe the structural organization and mechanical properties of viruses, including virus particles and infected cells across a wide range of spatial scales. We discuss the working principles of imaging procedures and analyses, and showcase how they open new avenues in virology. Finally, we discuss orthogonal approaches that enhance and complement label-free microscopy techniques. Mini Abstract Label-free imaging gives unprecedented insight into viruses at macroscopic, molecular and atomic levels. We present the major label-free imaging techniques and discuss how they are used for virus particles and infected cells. The power of label-free microscopy promises to enhance discovery of unknown aspects of infectious and therapeutic agents.

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How binding to surfaces affects disorder?

Cited by 3 publications

References 273 publications

Intrinsic Disorder in α-Synuclein Regulates the Exocytotic Fusion Pore Transition

Intrinsic Disorder in α-Synuclein Regulates the Exocytotic Fusion Pore Transition

Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure

Label-free microscopy for virus infections

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