Pub Date : 2025-03-20DOI: 10.1016/j.cbpa.2025.102585
Priscilla Dzigba , Megan A. Seth , Mallary C. Greenlee-Wacker , Benjamin M. Swarts
The increasing prevalence of antibiotic resistance, the stagnation of antibiotic development, and the adaptive capacity of bacteria to subvert the host immune response combine to pose significant global health concerns. Consequently, there is an urgent need to develop alternative therapeutic approaches to combat bacterial infections. Antibody-recruiting molecules (ARMs), which are bispecific small molecules that recruit endogenous antibodies to pathogenic cells or viruses, offer a promising avenue to harness the host immune system to target various diseases. In this review, we cover ARM strategies that have been developed for bacterial pathogens, including Gram-positive bacteria, Gram-negative bacteria, and mycobacteria, and we discuss the prospects and challenges of utilizing ARMs as alternatives to traditional antibiotic therapies.
{"title":"Redirecting the host immune response to bacterial infection with antibody-recruiting molecules (ARMs)","authors":"Priscilla Dzigba , Megan A. Seth , Mallary C. Greenlee-Wacker , Benjamin M. Swarts","doi":"10.1016/j.cbpa.2025.102585","DOIUrl":"10.1016/j.cbpa.2025.102585","url":null,"abstract":"<div><div>The increasing prevalence of antibiotic resistance, the stagnation of antibiotic development, and the adaptive capacity of bacteria to subvert the host immune response combine to pose significant global health concerns. Consequently, there is an urgent need to develop alternative therapeutic approaches to combat bacterial infections. Antibody-recruiting molecules (ARMs), which are bispecific small molecules that recruit endogenous antibodies to pathogenic cells or viruses, offer a promising avenue to harness the host immune system to target various diseases. In this review, we cover ARM strategies that have been developed for bacterial pathogens, including Gram-positive bacteria, Gram-negative bacteria, and mycobacteria, and we discuss the prospects and challenges of utilizing ARMs as alternatives to traditional antibiotic therapies.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"86 ","pages":"Article 102585"},"PeriodicalIF":6.9,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143673084","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 : 2025-03-12DOI: 10.1016/j.cbpa.2025.102584
Sigridur G. Suman
Functional mimics of enzymes have a long history with bioinorganic chemists. Early motivation for creating these mimics was strongly based on the study of the enzyme reaction mechanisms. In more recent times, interest in functional mimics has expanded to catalytic metallodrugs, where the mimics are deliberately designed for specific catalytic reactions intended for therapeutic purposes. In vivo, noncytotoxic catalysis targets reactions designed to activate prodrugs. Natural or de novo proteins were developed for artificial enzyme catalysis of Diels–Alder reactions, or as artificial oxygenase mimics. Novel sulfur-rich catalytic superoxide dismutase (SOD) mimics were discovered as antioxidants. Detoxification of elevated levels of cyanide where the natural rhodanese enzyme becomes inefficient in turnover rates and bioavailability is particularly attractive for sulfur-rich molybdenum clusters. This brief overview includes metal catalysts performing abiotic reactions in vivo disguised by attachment to cell surfaces, as artificial enzymes, and interesting new sulfur-rich complexes performing SOD reactions or neutralizing cyanide.
{"title":"Noncytotoxic catalytic enzyme functional mimics including cyanide poisoning antidotes","authors":"Sigridur G. Suman","doi":"10.1016/j.cbpa.2025.102584","DOIUrl":"10.1016/j.cbpa.2025.102584","url":null,"abstract":"<div><div>Functional mimics of enzymes have a long history with bioinorganic chemists. Early motivation for creating these mimics was strongly based on the study of the enzyme reaction mechanisms. In more recent times, interest in functional mimics has expanded to catalytic metallodrugs, where the mimics are deliberately designed for specific catalytic reactions intended for therapeutic purposes. <em>In vivo,</em> noncytotoxic catalysis targets reactions designed to activate prodrugs. Natural or <em>de novo</em> proteins were developed for artificial enzyme catalysis of Diels–Alder reactions, or as artificial oxygenase mimics. Novel sulfur-rich catalytic superoxide dismutase (SOD) mimics were discovered as antioxidants. Detoxification of elevated levels of cyanide where the natural rhodanese enzyme becomes inefficient in turnover rates and bioavailability is particularly attractive for sulfur-rich molybdenum clusters. This brief overview includes metal catalysts performing abiotic reactions <em>in vivo</em> disguised by attachment to cell surfaces, as artificial enzymes, and interesting new sulfur-rich complexes performing SOD reactions or neutralizing cyanide.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"86 ","pages":"Article 102584"},"PeriodicalIF":6.9,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143609929","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 : 2025-03-03DOI: 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}
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