Pub Date : 2025-03-03DOI: 10.1016/j.cbpa.2025.102582
Sandip Chattopadhayay, Pinaki Talukdar
Nature endowed different structurally and functionally complex transmembrane transporters to flux the ions to maintain the healthy functions of the cells by turning on or turning off the ion flow in the presence of external stimuli. Mimicking this stimuli-responsive behavior of natural transporters using synthetic analogs is currently an ongoing interest in the scientific community. This short review highlights the recent development of synthetic responsive ionophore systems. This includes pH, light, redox, enzyme, and multi-stimuli-controlled ionophores systems that have the potential to be utilized in different biomedical applications ranging from antibacterial activity to anticancer activity.
{"title":"Stimuli-responsive synthetic ionophores for therapeutic applications","authors":"Sandip Chattopadhayay, Pinaki Talukdar","doi":"10.1016/j.cbpa.2025.102582","DOIUrl":"10.1016/j.cbpa.2025.102582","url":null,"abstract":"<div><div>Nature endowed different structurally and functionally complex transmembrane transporters to flux the ions to maintain the healthy functions of the cells by turning on or turning off the ion flow in the presence of external stimuli. Mimicking this stimuli-responsive behavior of natural transporters using synthetic analogs is currently an ongoing interest in the scientific community. This short review highlights the recent development of synthetic responsive ionophore systems. This includes pH, light, redox, enzyme, and multi-stimuli-controlled ionophores systems that have the potential to be utilized in different biomedical applications ranging from antibacterial activity to anticancer activity.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102582"},"PeriodicalIF":6.9,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143534456","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-26DOI: 10.1016/j.cbpa.2025.102583
Anokhi Shah , Joshua L. Wort , Yue Ma , Christos Pliotas
{"title":"Corrigendum to “Enabling structural biological electron paramagnetic resonance spectroscopy in membrane proteins through spin labelling” Curr Opin Chem Biol 84 (2025) 102564","authors":"Anokhi Shah , Joshua L. Wort , Yue Ma , Christos Pliotas","doi":"10.1016/j.cbpa.2025.102583","DOIUrl":"10.1016/j.cbpa.2025.102583","url":null,"abstract":"","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102583"},"PeriodicalIF":6.9,"publicationDate":"2025-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143487537","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-19DOI: 10.1016/j.cbpa.2025.102581
Helene Jahn , Show-Ling Shyng , Carsten Schultz
Lipids can have specific interaction partners and act as small molecule regulators of proteins, especially for transmembrane proteins. Transmembrane proteins, such as ion channels, can be influenced by lipids in four ways; lipids can be direct ligands, localize effector proteins or domains, affect protein–protein interaction, or change the biophysical properties of the surrounding membrane. In this article, we will give examples of how lipids directly interact with ion channels and address the complex aspect of indirect regulation via lipids of the surrounding membrane bilayer. In addition, we discuss current and propose future molecular tools and experiments elucidating the many roles lipids play in ion channel function.
{"title":"Lipid probes to study ion channels","authors":"Helene Jahn , Show-Ling Shyng , Carsten Schultz","doi":"10.1016/j.cbpa.2025.102581","DOIUrl":"10.1016/j.cbpa.2025.102581","url":null,"abstract":"<div><div>Lipids can have specific interaction partners and act as small molecule regulators of proteins, especially for transmembrane proteins. Transmembrane proteins, such as ion channels, can be influenced by lipids in four ways; lipids can be direct ligands, localize effector proteins or domains, affect protein–protein interaction, or change the biophysical properties of the surrounding membrane. In this article, we will give examples of how lipids directly interact with ion channels and address the complex aspect of indirect regulation via lipids of the surrounding membrane bilayer. In addition, we discuss current and propose future molecular tools and experiments elucidating the many roles lipids play in ion channel function.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102581"},"PeriodicalIF":6.9,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143445707","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-17DOI: 10.1016/j.cbpa.2025.102570
Moriah Jospe-Kaufman, Micha Fridman
The rise in fungal infections, driven by pathogens resistant to the limited scope of antifungal agents available, poses an increasing threat to global health and the economy. Addressing this challenge requires a thorough understanding of the mechanisms of antifungal agents and the development of advanced resistance diagnostic methods. This opinion manuscript highlights recent advancements in antifungal research, with a focus on chemical biology approaches, particularly the development of fluorescent probes derived from various antifungal agents. These probes reveal new aspects of antifungal activity and provide deeper insights into modes of action and resistance mechanisms. Live cell imaging of fungal pathogens labeled with these probes has uncovered novel strategies to enhance antifungal efficacy, understand virulence factors, and detect resistance. These unique small-molecule tools offer powerful new avenues for addressing the fungal infections crisis, harnessing chemical biology approaches to develop innovative solutions to the global challenges posed by fungi.
{"title":"Illuminating antifungal mode of action and resistance with fluorescent probes","authors":"Moriah Jospe-Kaufman, Micha Fridman","doi":"10.1016/j.cbpa.2025.102570","DOIUrl":"10.1016/j.cbpa.2025.102570","url":null,"abstract":"<div><div>The rise in fungal infections, driven by pathogens resistant to the limited scope of antifungal agents available, poses an increasing threat to global health and the economy. Addressing this challenge requires a thorough understanding of the mechanisms of antifungal agents and the development of advanced resistance diagnostic methods. This opinion manuscript highlights recent advancements in antifungal research, with a focus on chemical biology approaches, particularly the development of fluorescent probes derived from various antifungal agents. These probes reveal new aspects of antifungal activity and provide deeper insights into modes of action and resistance mechanisms. Live cell imaging of fungal pathogens labeled with these probes has uncovered novel strategies to enhance antifungal efficacy, understand virulence factors, and detect resistance. These unique small-molecule tools offer powerful new avenues for addressing the fungal infections crisis, harnessing chemical biology approaches to develop innovative solutions to the global challenges posed by fungi.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102570"},"PeriodicalIF":6.9,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143427599","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-14DOI: 10.1016/j.cbpa.2025.102571
Hannah G. Addis , Erin E. Carlson
Bacterial infections, especially those that are resistant to antibiotics, constitute an increasing threat to public health. Deeper understanding about the systems that govern resistant infections, followed by the design of new therapies is crucial to minimizing morbidity and mortality due to antibacterial resistance. To this end, the discovery of small molecules capable of modulating bacterial processes is an important goal. Herein, we summarize recent developments in high-throughput screening, including the use of in vitro biochemical assays, reporter fusion read-out methods, and live cell phenotypic assays in bacteria. We also highlight key advantages and disadvantages of each assay type, as well as exciting new innovations.
{"title":"Recent advances in high-throughput screening methods for small molecule modulators in bacteria","authors":"Hannah G. Addis , Erin E. Carlson","doi":"10.1016/j.cbpa.2025.102571","DOIUrl":"10.1016/j.cbpa.2025.102571","url":null,"abstract":"<div><div>Bacterial infections, especially those that are resistant to antibiotics, constitute an increasing threat to public health. Deeper understanding about the systems that govern resistant infections, followed by the design of new therapies is crucial to minimizing morbidity and mortality due to antibacterial resistance. To this end, the discovery of small molecules capable of modulating bacterial processes is an important goal. Herein, we summarize recent developments in high-throughput screening, including the use of <em>in vitro</em> biochemical assays, reporter fusion read-out methods, and live cell phenotypic assays in bacteria. We also highlight key advantages and disadvantages of each assay type, as well as exciting new innovations.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102571"},"PeriodicalIF":6.9,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143420340","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-03DOI: 10.1016/j.cbpa.2025.102569
Tianlu Wang , Tatsuki Nonomura , Tien-Hung Lan , Yubin Zhou
Optogenetics, which integrates photonics and genetic engineering to control protein activity and cellular processes, has transformed biomedical research. Its precise spatiotemporal control, minimal invasiveness, and tunable reversibility have spurred its widespread adoption in both basic and clinical research. Optogenetic techniques have been applied to partially restore vision in blind patients and are being actively explored as innovative treatments for neurological, psychiatric, cardiac, and immunological disorders. Microbial channelrhodopsins (ChRs) allow precise manipulation of neuronal and cardiac activities, while vertebrate rhodopsins offer unique opportunities for ion channel modulation through G-protein-coupled receptor (GPCR) pathways. Plant-derived photoswitchable domains can also be engineered into ion channels to confer photosensitivity. This review summarizes the latest progress in engineering genetically encoded light-sensitive ion channel actuators and modulators (GELICAMs) with diverse ion selectivity and spectral sensitivity. We further discuss the potential applications and challenges of these tools in advancing biomedical research and therapeutic interventions.
{"title":"Optogenetic engineering for ion channel modulation","authors":"Tianlu Wang , Tatsuki Nonomura , Tien-Hung Lan , Yubin Zhou","doi":"10.1016/j.cbpa.2025.102569","DOIUrl":"10.1016/j.cbpa.2025.102569","url":null,"abstract":"<div><div>Optogenetics, which integrates photonics and genetic engineering to control protein activity and cellular processes, has transformed biomedical research. Its precise spatiotemporal control, minimal invasiveness, and tunable reversibility have spurred its widespread adoption in both basic and clinical research. Optogenetic techniques have been applied to partially restore vision in blind patients and are being actively explored as innovative treatments for neurological, psychiatric, cardiac, and immunological disorders. Microbial channelrhodopsins (ChRs) allow precise manipulation of neuronal and cardiac activities, while vertebrate rhodopsins offer unique opportunities for ion channel modulation through G-protein-coupled receptor (GPCR) pathways. Plant-derived photoswitchable domains can also be engineered into ion channels to confer photosensitivity. This review summarizes the latest progress in engineering genetically encoded light-sensitive ion channel actuators and modulators (GELICAMs) with diverse ion selectivity and spectral sensitivity. We further discuss the potential applications and challenges of these tools in advancing biomedical research and therapeutic interventions.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"85 ","pages":"Article 102569"},"PeriodicalIF":6.9,"publicationDate":"2025-02-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143132999","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-01DOI: 10.1016/j.cbpa.2024.102553
Ashlee E. Wertz , Hannah S. Shafaat
Enzymes catalyze molecular reactions with remarkable efficiency and selectivity under mild conditions. Photoactivated enzymes make use of a light-absorbing chromophore to drive chemical transformations, ideally using sunlight as an energy source. The direct attachment of a chromophore to native enzymes is advantageous, as information on the underlying catalytic mechanisms can be obtained. Artificial enzyme development seeks to mimic natural enzymes to generate valuable products with high efficiency in a simplified, robust framework. Light-initiated artificial enzymatic catalysis combines these strategies and represents a promising avenue for sustainable generation of value-added products. Furthermore, while early systems often combined three components for catalysis-- the enzyme, a photosensitizer, and a sacrificial electron donor-- we describe an adaptation of this approach in which the chromophore is immobilized on the enzyme, removing the need for diffusional collision. The latter is advantageous as it provides deeper insight into the catalytic mechanism and facilitates further optimization of the designed construct. In this opinion, we highlight several examples of light-driven, artificial metalloenzymes, and suggest that ongoing and future efforts should leverage prior mechanistic studies on native enzymes as a foundation for strategic design of next-generation photoactivated protein-based catalysts.
{"title":"Developing photoactivated artificial enzymes for sustainable fuel production","authors":"Ashlee E. Wertz , Hannah S. Shafaat","doi":"10.1016/j.cbpa.2024.102553","DOIUrl":"10.1016/j.cbpa.2024.102553","url":null,"abstract":"<div><div>Enzymes catalyze molecular reactions with remarkable efficiency and selectivity under mild conditions. Photoactivated enzymes make use of a light-absorbing chromophore to drive chemical transformations, ideally using sunlight as an energy source. The direct attachment of a chromophore to native enzymes is advantageous, as information on the underlying catalytic mechanisms can be obtained. Artificial enzyme development seeks to mimic natural enzymes to generate valuable products with high efficiency in a simplified, robust framework. Light-initiated artificial enzymatic catalysis combines these strategies and represents a promising avenue for sustainable generation of value-added products. Furthermore, while early systems often combined three components for catalysis-- the enzyme, a photosensitizer, and a sacrificial electron donor-- we describe an adaptation of this approach in which the chromophore is immobilized on the enzyme, removing the need for diffusional collision. The latter is advantageous as it provides deeper insight into the catalytic mechanism and facilitates further optimization of the designed construct. In this opinion, we highlight several examples of light-driven, artificial metalloenzymes, and suggest that ongoing and future efforts should leverage prior mechanistic studies on native enzymes as a foundation for strategic design of next-generation photoactivated protein-based catalysts.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102553"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142906428","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-01DOI: 10.1016/j.cbpa.2024.102562
Amr M. El-Araby, Jed F. Fisher, Shahriar Mobashery
The peptidoglycan manifests as a multifaceted component of the bacterial cell wall. Throughout the lifecycle of the bacterium, the peptidoglycan is deconstructed, rebuilt, and remodeled for bacterial cell growth and replication. Degradation products of the peptidoglycan serve as precursors for cell-wall building blocks via recycling processes and as signaling molecules. Cell-wall recycling and de novo cell-wall synthesis converge biochemically at the cytoplasmic compartment. Peptidoglycan biochemistry is finely tuned to maintain the polymer's functions and is intimately connected to antibiotic-resistance mechanisms. Cell-wall-modifying enzymes present a unique opportunity for the discovery of antibiotics and antibiotic adjuvants. The unique chemical template of the peptidoglycan has been a target of numerous chemical biology approaches for investigating its functions and modulation. In this review, we highlight the current perspective on peptidoglycan research. We present recent efforts to understand the peptidoglycan as a functional component of antibiotic resistance, and as a target for antimicrobial therapy.
{"title":"Bacterial peptidoglycan as a living polymer","authors":"Amr M. El-Araby, Jed F. Fisher, Shahriar Mobashery","doi":"10.1016/j.cbpa.2024.102562","DOIUrl":"10.1016/j.cbpa.2024.102562","url":null,"abstract":"<div><div>The peptidoglycan manifests as a multifaceted component of the bacterial cell wall. Throughout the lifecycle of the bacterium, the peptidoglycan is deconstructed, rebuilt, and remodeled for bacterial cell growth and replication. Degradation products of the peptidoglycan serve as precursors for cell-wall building blocks <em>via</em> recycling processes and as signaling molecules. Cell-wall recycling and <em>de novo</em> cell-wall synthesis converge biochemically at the cytoplasmic compartment. Peptidoglycan biochemistry is finely tuned to maintain the polymer's functions and is intimately connected to antibiotic-resistance mechanisms. Cell-wall-modifying enzymes present a unique opportunity for the discovery of antibiotics and antibiotic adjuvants. The unique chemical template of the peptidoglycan has been a target of numerous chemical biology approaches for investigating its functions and modulation. In this review, we highlight the current perspective on peptidoglycan research. We present recent efforts to understand the peptidoglycan as a functional component of antibiotic resistance, and as a target for antimicrobial therapy.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102562"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142862589","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-01DOI: 10.1016/j.cbpa.2024.102548
Mariah A. Cook , Shelby M. Phelps , Jasmine N. Tutol , Derik A. Adams, Sheel C. Dodani
Anions are critical to all life forms. Anions can be absorbed as nutrients or biosynthesized. Anions shape a spectrum of fundamental biological processes at the organismal, cellular, and subcellular scales. Genetically encoded fluorescent biosensors can capture anions in action across time and space dimensions with microscopy. The firsts of such technologies were reported more than 20 years for monoatomic chloride and polyatomic cAMP anions. However, the recent boom of anion biosensors illuminates the unknowns and opportunities that remain for toolmakers and end users to meet across the aisle to spur innovations in biosensor designs and applications for discovery anion biology. In this review, we will canvas progress made over the last three years for biologically relevant anions that are classified as halides, oxyanions, carboxylates, and nucleotides.
{"title":"Illuminating anions in biology with genetically encoded fluorescent biosensors","authors":"Mariah A. Cook , Shelby M. Phelps , Jasmine N. Tutol , Derik A. Adams, Sheel C. Dodani","doi":"10.1016/j.cbpa.2024.102548","DOIUrl":"10.1016/j.cbpa.2024.102548","url":null,"abstract":"<div><div>Anions are critical to all life forms. Anions can be absorbed as nutrients or biosynthesized. Anions shape a spectrum of fundamental biological processes at the organismal, cellular, and subcellular scales. Genetically encoded fluorescent biosensors can capture anions in action across time and space dimensions with microscopy. The firsts of such technologies were reported more than 20 years for monoatomic chloride and polyatomic cAMP anions. However, the recent boom of anion biosensors illuminates the unknowns and opportunities that remain for toolmakers and end users to meet across the aisle to spur innovations in biosensor designs and applications for discovery anion biology. In this review, we will canvas progress made over the last three years for biologically relevant anions that are classified as halides, oxyanions, carboxylates, and nucleotides.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102548"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142805597","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-01DOI: 10.1016/j.cbpa.2024.102564
Anokhi Shah , Joshua L. Wort , Yue Ma , Christos Pliotas
Pulsed dipolar electron paramagnetic resonance spectroscopy (PDS), combined with site-directed spin-labelling, represents a powerful tool for the investigation of biomacromolecules, emerging as a keystone approach in structural biology. Increasingly, PDS is applied to study highly complex integral membrane protein systems, such as mechanosensitive ion channels, transporters, G-protein coupled receptors, ion pumps, and outer membrane proteins elucidating their dynamics and revealing conformational ensembles. Indeed, PDS offers a platform to study intermediate or lowly-populated states that are otherwise invisible to other modern methods, such as X-ray crystallography, cryo-EM, and hydrogen-deuterium exchange-mass spectrometry. Importantly, advances in spin labelling strategies welcome a new era of membrane protein investigation under near-native or in-cell conditions. Here, we review recent integral membrane protein PDS applications, and highlight well-suited, emerging spin labelling strategies that show promise for future studies.
{"title":"Enabling structural biological electron paramagnetic resonance spectroscopy in membrane proteins through spin labelling","authors":"Anokhi Shah , Joshua L. Wort , Yue Ma , Christos Pliotas","doi":"10.1016/j.cbpa.2024.102564","DOIUrl":"10.1016/j.cbpa.2024.102564","url":null,"abstract":"<div><div>Pulsed dipolar electron paramagnetic resonance spectroscopy (PDS), combined with site-directed spin-labelling, represents a powerful tool for the investigation of biomacromolecules, emerging as a keystone approach in structural biology. Increasingly, PDS is applied to study highly complex integral membrane protein systems, such as mechanosensitive ion channels, transporters, G-protein coupled receptors, ion pumps, and outer membrane proteins elucidating their dynamics and revealing conformational ensembles. Indeed, PDS offers a platform to study intermediate or lowly-populated states that are otherwise invisible to other modern methods, such as X-ray crystallography, cryo-EM, and hydrogen-deuterium exchange-mass spectrometry. Importantly, advances in spin labelling strategies welcome a new era of membrane protein investigation under near-native or in-cell conditions. Here, we review recent integral membrane protein PDS applications, and highlight well-suited, emerging spin labelling strategies that show promise for future studies.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102564"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142875665","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
扫码关注我们
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号