Identification of a critical lipid ratio in raft-like phases exposed to nitric oxide: An AFM study

Karanth, Sanjai; Azinfar, Amir; Helm, Christiane A.; Delcea, Mihaela

doi:10.1016/j.bpj.2021.06.009

Cited by 4 publications

(3 citation statements)

References 58 publications

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“…Such questions can now be answered using the NDs approach in combination with AFM, which will provide information about changes in membrane elasticity and permeability. Such quantitative analysis have been carried out previously on supported lipid bilayers . As mentioned earlier, determining the kinetics of protein–ligand interaction would provide explicit information about the metaphysical state of the protein.…”

Section: Addressing the Challenges In Flavor Research And Future Dire...mentioning

confidence: 98%

“…Such quantitative analysis have been carried out previously on supported lipid bilayers. 46 As mentioned earlier, determining the kinetics of protein−ligand interaction would provide explicit information about the metaphysical state of the protein. Identification of such intermediate steps is possible with techniques such as cryoEM or high-speed AFM.…”

Section: Research and Future Directionsmentioning

confidence: 99%

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Nanodisc Technology: Direction toward Physicochemical Characterization of Chemosensory Membrane Proteins in Food Flavor Research

Karanth,

Benthin,

Wiesenfarth

et al. 2024

J. Agric. Food Chem.

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Chemosensory membrane proteins such as G-protein-coupled receptors (GPCRs) drive flavor perception of food formulations. To achieve this, a detailed understanding of the structure and function of these membrane proteins is needed, which is often limited by the extraction and purification methods involved. The proposed nanodisc methodology helps overcome some of these existing challenges such as protein stability and solubilization along with their reconstitution from a native cell-membrane environment. Being well-established in structural biology procedures, nanodiscs offer this elegant solution by using, e.g., a membrane scaffold protein (MSP) or styrene−maleic acid (SMA) polymer, which interacts directly with the cell membrane during protein reconstitution. Such derived proteins retain their biophysical properties without compromising the membrane architecture. Here, we seek to show that these lipidic systems can be explored for insights with a focus on chemosensory membrane protein morphology and structure, conformational dynamics of protein−ligand interactions, and binding kinetics to answer pending questions in flavor research. Additionally, the compatibility of nanodiscs across varied (labeled or label-free) techniques offers significant leverage, which has been highlighted here.

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Section: Addressing the Challenges In Flavor Research And Future Dire...mentioning

confidence: 98%

Section: Research and Future Directionsmentioning

confidence: 99%

Nanodisc Technology: Direction toward Physicochemical Characterization of Chemosensory Membrane Proteins in Food Flavor Research

Karanth,

Benthin,

Wiesenfarth

et al. 2024

J. Agric. Food Chem.

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“…Concentration of sphingomyelin in the lipid rafts is higher than in non-raft portions of the membrane, where appropriate ratios in the lipid rafts is critical to face redox injuries, such as for example those caused by radicals such as nitric oxide-•NO [24].…”

Section: Ceramides As Structural Elements Of Biological Membranes As Well As Bioactive Moleculesmentioning

confidence: 99%

Plasma Ceramides Pathophysiology, Measurements, Challenges, and Opportunities

2021

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Ceramides are a family of lipid molecules, composed of sphingosine and a fatty acid, and transported by lipoproteins (primarily by low-density lipoproteins) in the bloodstream. They are not only structural lipids, but multifunctional and bioactive molecules with key roles in many important cellular pathways, such as inflammatory processes and apoptosis, representing potential biomarkers of cardiometabolic diseases as well as pharmacological targets. Recent data reported ceramide modulation by diet and aerobic exercise, suggesting nutrients and exercise-targeting sphingolipid pathways as a countermeasure, also in combination with other therapies, for risk and progression of chronic disease prevention and health maintenance. In this review, we focus on the available data regarding remarks on ceramide structure and metabolism, their pathophysiologic roles, and the effect of dietary habit and aerobic exercise on ceramide levels. Moreover, advancements and limitations of lipidomic techniques and simplification attempts to overcome difficulties of interpretation and to facilitate practical applications, such as the proposal of scores, are also discussed.

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The path to the G protein‐coupled receptor structural landscape: Major milestones and future directions

Kogut‐Günthel,

Zara,

Nicoli

et al. 2024

British J Pharmacology

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G protein‐coupled receptors (GPCRs) play a crucial role in cell function by transducing signals from the extracellular environment to the inside of the cell. They mediate the effects of various stimuli, including hormones, neurotransmitters, ions, photons, food tastants and odorants, and are renowned drug targets. Advancements in structural biology techniques, including X‐ray crystallography and cryo‐electron microscopy (cryo‐EM), have driven the elucidation of an increasing number of GPCR structures. These structures reveal novel features that shed light on receptor activation, dimerization and oligomerization, dichotomy between orthosteric and allosteric modulation, and the intricate interactions underlying signal transduction, providing insights into diverse ligand‐binding modes and signalling pathways. However, a substantial portion of the GPCR repertoire and their activation states remain structurally unexplored. Future efforts should prioritize capturing the full structural diversity of GPCRs across multiple dimensions. To do so, the integration of structural biology with biophysical and computational techniques will be essential. We describe in this review the progress of nuclear magnetic resonance (NMR) to examine GPCR plasticity and conformational dynamics, of atomic force microscopy (AFM) to explore the spatial–temporal dynamics and kinetic aspects of GPCRs, and the recent breakthroughs in artificial intelligence for protein structure prediction to characterize the structures of the entire GPCRome. In summary, the journey through GPCR structural biology provided in this review illustrates how far we have come in decoding these essential proteins architecture and function. Looking ahead, integrating cutting‐edge biophysics and computational tools offers a path to navigating the GPCR structural landscape, ultimately advancing GPCR‐based applications.

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Identification of a critical lipid ratio in raft-like phases exposed to nitric oxide: An AFM study

Cited by 4 publications

References 58 publications

Nanodisc Technology: Direction toward Physicochemical Characterization of Chemosensory Membrane Proteins in Food Flavor Research

Nanodisc Technology: Direction toward Physicochemical Characterization of Chemosensory Membrane Proteins in Food Flavor Research

Plasma Ceramides Pathophysiology, Measurements, Challenges, and Opportunities

The path to the G protein‐coupled receptor structural landscape: Major milestones and future directions

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