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}
Pub Date : 2025-02-01DOI: 10.1016/j.cbpa.2024.102566
Joel W.H. Wong , Emily P. Balskus
Bacteriophages (phages) play a critical role in microbial ecology and evolution. Their interactions with bacteria are influenced by a complex network of chemical signals derived from a wide range of sources including both endogenous bacterial metabolites and exogenous environmental compounds. In this review, we highlight two areas where small molecules play a pivotal role in modulating phage behaviors. First, we discuss how temperate phages respond to various chemical cues that influence the lysis-lysogeny decision, describing recent advances in our understanding of noncanonical cues. Second, we examine the diverse array of small molecules that disrupt phage infection, potentially serving as bacterial defense strategies against their long-standing competitors. Collectively, this growing body of research highlights the intricate molecular mechanisms governing phage-bacteria dynamics, offering new perspectives on the chemical language shaping microbial communities.
{"title":"Small molecules as modulators of phage–bacteria interactions","authors":"Joel W.H. Wong , Emily P. Balskus","doi":"10.1016/j.cbpa.2024.102566","DOIUrl":"10.1016/j.cbpa.2024.102566","url":null,"abstract":"<div><div>Bacteriophages (phages) play a critical role in microbial ecology and evolution. Their interactions with bacteria are influenced by a complex network of chemical signals derived from a wide range of sources including both endogenous bacterial metabolites and exogenous environmental compounds. In this review, we highlight two areas where small molecules play a pivotal role in modulating phage behaviors. First, we discuss how temperate phages respond to various chemical cues that influence the lysis-lysogeny decision, describing recent advances in our understanding of noncanonical cues. Second, we examine the diverse array of small molecules that disrupt phage infection, potentially serving as bacterial defense strategies against their long-standing competitors. Collectively, this growing body of research highlights the intricate molecular mechanisms governing phage-bacteria dynamics, offering new perspectives on the chemical language shaping microbial communities.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102566"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142906429","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.2024.102552
Sheng Zhao , Na Yu , Hesong Han , Shutao Guo , Niren Murthy
Drug delivery vectors have the potential to improve the efficacy of therapeutics, including small molecules and nucleic acid-based drugs. However, challenges remain in developing linkages that enable the precise and efficient release of therapeutic cargo in response to mildly acidic environments or lysosomal enzymes. This review highlights recent advances in acid-degradable acetal/ketal and enzyme-cleavable linkages for endolysosomal release. These innovations include the developments of azido-acetal linkers with improved stability and hydrolysis kinetics, organocatalytic trans-isopropenylation for synthesizing asymmetric ketals and their applications in drug delivery, and enzyme-cleavable linkers activated by cathepsin B or β-galactosidase.
{"title":"Advances in acid-degradable and enzyme-cleavable linkers for drug delivery","authors":"Sheng Zhao , Na Yu , Hesong Han , Shutao Guo , Niren Murthy","doi":"10.1016/j.cbpa.2024.102552","DOIUrl":"10.1016/j.cbpa.2024.102552","url":null,"abstract":"<div><div>Drug delivery vectors have the potential to improve the efficacy of therapeutics, including small molecules and nucleic acid-based drugs. However, challenges remain in developing linkages that enable the precise and efficient release of therapeutic cargo in response to mildly acidic environments or lysosomal enzymes. This review highlights recent advances in acid-degradable acetal/ketal and enzyme-cleavable linkages for endolysosomal release. These innovations include the developments of azido-acetal linkers with improved stability and hydrolysis kinetics, organocatalytic trans-isopropenylation for synthesizing asymmetric ketals and their applications in drug delivery, and enzyme-cleavable linkers activated by cathepsin B or <em>β</em>-galactosidase.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102552"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142789441","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}
Animal venom contains ion channel-targeting peptide toxins that inflict paralysis or pain. The high specificity and potency of these toxins for their target ion channels provides enticing opportunities for their deployment as tools in channel biology. Mechanistic studies on toxin-mediated ion channel modulation have yielded landmark breakthroughs in our understanding of channel architectures and gating mechanisms. Toxins have been recently repurposed as powerful structural biology probes to obtain structures of ion channels in elusive toxin-stabilized conformations providing unprecedented insights into channel gating. Insightful glimpses of protein–lipid interactions provided by some of these structures have served as blueprints for electrophysiology-based studies aimed at elucidating the functional roles of these interactions. Moreover, toxins appended with fluorophores have been used for clinical, biophysical, and cell biology-based studies. Herein, we summarize the contributions of ion channel-targeting toxins as tools in voltage-gated ion channel and transient receptor potential channel biology.
{"title":"Peptide toxins as tools in ion channel biology","authors":"Sucheta Bandyopadhyay , Satyajit Mishra , Jeet Kalia","doi":"10.1016/j.cbpa.2024.102568","DOIUrl":"10.1016/j.cbpa.2024.102568","url":null,"abstract":"<div><div>Animal venom contains ion channel-targeting peptide toxins that inflict paralysis or pain. The high specificity and potency of these toxins for their target ion channels provides enticing opportunities for their deployment as tools in channel biology. Mechanistic studies on toxin-mediated ion channel modulation have yielded landmark breakthroughs in our understanding of channel architectures and gating mechanisms. Toxins have been recently repurposed as powerful structural biology probes to obtain structures of ion channels in elusive toxin-stabilized conformations providing unprecedented insights into channel gating. Insightful glimpses of protein–lipid interactions provided by some of these structures have served as blueprints for electrophysiology-based studies aimed at elucidating the functional roles of these interactions. Moreover, toxins appended with fluorophores have been used for clinical, biophysical, and cell biology-based studies. Herein, we summarize the contributions of ion channel-targeting toxins as tools in voltage-gated ion channel and transient receptor potential channel biology.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102568"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142925853","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.2024.102565
Zhe Zhou , Stavroula K. Hatzios
Humans are exposed to a wide variety of small molecules with antioxidant properties that are poorly metabolized by mammalian cells. However, gastrointestinal microbes encode enzymes that convert these redox-active molecules into nutrient sources and electron acceptors to support bacterial growth in the gut. Here, we describe recent studies highlighting how microbial metabolism of host-derived antioxidants modulates interspecies interactions and provide an overview of the interdisciplinary approaches being used to map these metabolic pathways in vivo. Uncovering microbe-driven biotransformations of redox-active small molecules could create new opportunities to improve human health by modulating redox reactions at the host–microbe interface.
{"title":"Microbial metabolism of host-derived antioxidants","authors":"Zhe Zhou , Stavroula K. Hatzios","doi":"10.1016/j.cbpa.2024.102565","DOIUrl":"10.1016/j.cbpa.2024.102565","url":null,"abstract":"<div><div>Humans are exposed to a wide variety of small molecules with antioxidant properties that are poorly metabolized by mammalian cells. However, gastrointestinal microbes encode enzymes that convert these redox-active molecules into nutrient sources and electron acceptors to support bacterial growth in the gut. Here, we describe recent studies highlighting how microbial metabolism of host-derived antioxidants modulates interspecies interactions and provide an overview of the interdisciplinary approaches being used to map these metabolic pathways <em>in vivo</em>. Uncovering microbe-driven biotransformations of redox-active small molecules could create new opportunities to improve human health by modulating redox reactions at the host–microbe interface.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102565"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142890863","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.2024.102567
Ran Tivony
Natural ion channels have long inspired the design of synthetic nanopores with protein-like features. A significant leap towards this endeavor has been made possible using DNA origami. The exploitation of DNA as a building material has enabled the construction of biomimetic DNA nanopores with a range of pore dimensions and stimuli-responsive capabilities. However, structural fluctuations and ion leakage across the walls of DNA nanopores greatly limit their use in various applications like label-free sensing and as a research tool in functional studies of ion channels. This review outlines some of the guiding principles for biomimetic engineering of DNA-based ion channels, discusses the weaknesses of current DNA nanopore designs, and presents recent efforts to alleviate these limitations.
{"title":"Synthetic ion channels made of DNA","authors":"Ran Tivony","doi":"10.1016/j.cbpa.2024.102567","DOIUrl":"10.1016/j.cbpa.2024.102567","url":null,"abstract":"<div><div>Natural ion channels have long inspired the design of synthetic nanopores with protein-like features. A significant leap towards this endeavor has been made possible using DNA origami. The exploitation of DNA as a building material has enabled the construction of biomimetic DNA nanopores with a range of pore dimensions and stimuli-responsive capabilities. However, structural fluctuations and ion leakage across the walls of DNA nanopores greatly limit their use in various applications like label-free sensing and as a research tool in functional studies of ion channels. This review outlines some of the guiding principles for biomimetic engineering of DNA-based ion channels, discusses the weaknesses of current DNA nanopore designs, and presents recent efforts to alleviate these limitations.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102567"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142913235","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.2024.102547
Alicia Climent-Catala, Mateo I. Sanchez
Intracellular calcium (Ca2+) is involved in a plethora of cell signalling processes and physiological functions. Increases in Ca2+ concentration are bona fide biomarkers of neuronal activity, reflecting the spike count, timing, frequency, and the intensity of synaptic input. The development of genetically encoded calcium indicators (GECIs) was a significant advancement in modern neuroscience that enabled real-time visualisation of neuronal activity at single-cell resolution. These indicators leverage the conformational changes induced by calcium-binding proteins, such as calmodulin (CaM) or troponin C (TnC). Harnessing protein engineering approaches such as directed evolution yielded new GECIs with enhanced sensitivity, kinetics, and brightness. Notably, the development of calcium-based integrators, such as scFLARE (single-chain fast light- and activity-regulated expression), convert transient raises in cytosolic Ca2+ into a transcriptional readout rather than an optical signal. This review summarises the latest efforts in protein engineering to develop new indicators and molecular systems to sense changes in Ca2+ concentrations.
{"title":"Development of novel indicators and molecular systems for calcium sensing through protein engineering","authors":"Alicia Climent-Catala, Mateo I. Sanchez","doi":"10.1016/j.cbpa.2024.102547","DOIUrl":"10.1016/j.cbpa.2024.102547","url":null,"abstract":"<div><div>Intracellular calcium (Ca<sup>2+</sup>) is involved in a plethora of cell signalling processes and physiological functions. Increases in Ca<sup>2+</sup> concentration are <em>bona fide</em> biomarkers of neuronal activity, reflecting the spike count, timing, frequency, and the intensity of synaptic input. The development of genetically encoded calcium indicators (GECIs) was a significant advancement in modern neuroscience that enabled real-time visualisation of neuronal activity at single-cell resolution. These indicators leverage the conformational changes induced by calcium-binding proteins, such as calmodulin (CaM) or troponin C (TnC). Harnessing protein engineering approaches such as directed evolution yielded new GECIs with enhanced sensitivity, kinetics, and brightness. Notably, the development of calcium-based integrators, such as scFLARE (single-chain fast light- and activity-regulated expression), convert transient raises in cytosolic Ca<sup>2+</sup> into a transcriptional readout rather than an optical signal. This review summarises the latest efforts in protein engineering to develop new indicators and molecular systems to sense changes in Ca<sup>2+</sup> concentrations.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102547"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142783566","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 : 2025-02-01DOI: 10.1016/j.cbpa.2024.102563
Manuel Pérez-Pérez, Alberto Fuertes, Javier Montenegro
Transmembrane ion exchange controls biological functions and is essential for life. Over the years, a great variety of nature-inspired artificial ion channels and carriers have been synthesized to control and promote ion exchange across biological membranes. In this context, peptides emerged as ideal scaffolds for synthetic ion channels due to their biocompatibility, accessibility and chemical versatility. Peptides have already shown their potential for the construction of a range of synthetic ion transporters either alone or in combination with other molecular scaffolds. Among the great diversity of peptide-based ion transporters, we can find key examples of single-molecule and supramolecular transmembrane ion channels and ionophores. Peptide scaffolds have also found great potential for the transmembrane delivery of biomolecular cargos such as nucleic acids and proteins. This review covers some of the most relevant advances in the peptide-based ion transport field from the last few years.
{"title":"Synthetic peptide scaffolds as ion channels and molecular carriers","authors":"Manuel Pérez-Pérez, Alberto Fuertes, Javier Montenegro","doi":"10.1016/j.cbpa.2024.102563","DOIUrl":"10.1016/j.cbpa.2024.102563","url":null,"abstract":"<div><div>Transmembrane ion exchange controls biological functions and is essential for life. Over the years, a great variety of nature-inspired artificial ion channels and carriers have been synthesized to control and promote ion exchange across biological membranes. In this context, peptides emerged as ideal scaffolds for synthetic ion channels due to their biocompatibility, accessibility and chemical versatility. Peptides have already shown their potential for the construction of a range of synthetic ion transporters either alone or in combination with other molecular scaffolds. Among the great diversity of peptide-based ion transporters, we can find key examples of single-molecule and supramolecular transmembrane ion channels and ionophores. Peptide scaffolds have also found great potential for the transmembrane delivery of biomolecular cargos such as nucleic acids and proteins. This review covers some of the most relevant advances in the peptide-based ion transport field from the last few years.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102563"},"PeriodicalIF":6.9,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142942112","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 : 2024-11-30DOI: 10.1016/j.cbpa.2024.102549
Iqra Zubair , Luis Martínez-Crespo , Simon J. Webb
Crucial physiological processes, like neural communication and muscle contraction, are mediated by protein channels in cell membranes. These natural channels typically have a central hydrophilic pore with tightly defined dimensions, which can be opened or closed (‘gated’) by external stimuli. Mimicking natural ion channels using synthetic molecules is a long-standing goal in artificial channel research. Although current synthetic channels have not yet achieved the same combination of high activity, high selectivity, and gating as natural channels, foldamers offer a new approach. Foldamers are unnatural oligomers that fold into defined three-dimensional shapes, similar to the way that natural polypeptides fold into secondary structures. With defined shapes and often multi-nanometre dimensions, foldamers have become valuable tools to mimic the behaviour of natural proteins in membranes. This review highlights selected recent examples of foldamer channels, examples that indicate how foldamer architectures may lead to controllable channels with high activity and selectivity.
{"title":"Foldamer-mediated transport across phospholipid bilayers","authors":"Iqra Zubair , Luis Martínez-Crespo , Simon J. Webb","doi":"10.1016/j.cbpa.2024.102549","DOIUrl":"10.1016/j.cbpa.2024.102549","url":null,"abstract":"<div><div>Crucial physiological processes, like neural communication and muscle contraction, are mediated by protein channels in cell membranes. These natural channels typically have a central hydrophilic pore with tightly defined dimensions, which can be opened or closed (‘gated’) by external stimuli. Mimicking natural ion channels using synthetic molecules is a long-standing goal in artificial channel research. Although current synthetic channels have not yet achieved the same combination of high activity, high selectivity, and gating as natural channels, foldamers offer a new approach. Foldamers are unnatural oligomers that fold into defined three-dimensional shapes, similar to the way that natural polypeptides fold into secondary structures. With defined shapes and often multi-nanometre dimensions, foldamers have become valuable tools to mimic the behaviour of natural proteins in membranes. This review highlights selected recent examples of foldamer channels, examples that indicate how foldamer architectures may lead to controllable channels with high activity and selectivity.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"84 ","pages":"Article 102549"},"PeriodicalIF":6.9,"publicationDate":"2024-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142746714","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}
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