Medicinal Chemistry Research最新文献

{"title":"Development of novel triconjugates fusing melatonin/isatin/N-acylhydrazone targeting colorectal cancer: design, synthesis, biological, and in silico ADME/Tox profiling","authors":"Sara M. Gutiérrez,&nbsp;Wilson Cardona-Galeano,&nbsp;Angie Herrera-Ramírez,&nbsp;Andres F. Yepes","doi":"10.1007/s00044-024-03358-1","DOIUrl":"10.1007/s00044-024-03358-1","url":null,"abstract":"<div><p>Herein, a new library of triconjugates linked melatonin with the biological active cores of isatin and <i>N</i>-acylhydrazone were designed, synthetized, and their biological activity was evaluated in human colorectal cancer cells. All compounds were screened to determine the potential at a single dose of 100 µM against human colon adenocarcinoma SW480 cells, finding one compound <b>3e</b> which caused 100% inhibition and a certain grade of lethality at the conditions evaluated. In addition, the most active and soluble hybrids were further assessed using a five-dose scheme in the same colon cancer cells, and non-malignant human colon epithelial cells (NCM460) to establish the selective potential, finding that hybridized molecules <b>3e</b>, <b>3g</b>, and <b>3l</b> were more cytotoxic than parental compounds and 4-fold more selective than the reference drug (5-fluorouracil, 5-FU) which shows that molecular hybridization remains as a valuable tool to produce novel chemical entities that may result in advances in medicine. Lastly, according to a theoretical analysis on drug-like properties, pharmacokinetics, and toxicology, for the most promising hybrid <b>3e</b> would show a strong possibility of moving on to further preclinical research. Our results clearly demonstrated the effectiveness of melatonin/isatin/<i>N</i>-acylhydrazone triconjugates, with the 2-hydroxyphenylsubstituted compound in particular serving as a prototype drug for future investigations into innovative therapeutic treatments for colorectal cancer.</p></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"648 - 663"},"PeriodicalIF":2.6,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143480874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis and anti-inflammatory activity of chromone-sulfonamide derivatives as COXs/iNOS dual-target inhibitors","authors":"Meng Qin,&nbsp;Tao Xing,&nbsp;Mengdi Zhang,&nbsp;Jiatong Han,&nbsp;Shuyan Yu,&nbsp;Jianping Chen,&nbsp;Yuheng Ma","doi":"10.1007/s00044-024-03368-z","DOIUrl":"10.1007/s00044-024-03368-z","url":null,"abstract":"<div><p>Cyclooxygenase and inducible nitric oxide synthase are key proteins in two different pathways that produce inflammation. In this study, we based on the principle of pharmacophore combination to obtain small molecules that can block the dual targets of COXs and iNOS. We screened two pharmacophores with anti-inflammatory activity, chromone ring and sulfonamide from clinical drugs, natural products and other compounds with outstanding biological activity, and synthesized 9 novel chromone-sulfonamide derivatives, among which compounds 4a, 4b, 4c, 4d and 4i exhibited different degrees of COXs and iNOS inhibition. In particular, compound 4i exhibited the most significant dual inhibitory effect, with an IC₅₀ of 28.83 ± 0.06 μM for PGE₂ and an IC₅₀ of 36.95 ± 3.9 μM for NO content, which was superior to the positive drugs ibuprofen (IBU, IC₅₀ = 246.5 ± 3.8 μM) and L-canavanine (L-Can., IC₅₀ = 440.0 ± 7.9 μM). In addition, the research group used Discovery Studio to dock the target compounds with COX-1, COX-2 and iNOS, respectively, and the results showed that compound 4i had the best docking method (its -CDOCK INTERACTION ENERGY scores were 48.2967, 45.3519 and 43.4412, respectively, which were better than those of other compounds), which was consistent with the results of activity experiments, and the chromone ring and sulfonamide group could form hydrogen bonds between the two target proteins, conjugation and van der Waals interactions, indicating that the chromone ring and sulfonamide group are key pharmacophores. In addition, a preliminary study of the structure-activity relationship of the compound was carried out to identify the key factors affecting the anti-inflammatory activity, and 4i matched the structure-activity relationship, which indicated that 4i was a lead compound for the development of dual COXs/iNOS inhibition for the treatment of inflammatory diseases.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"638 - 647"},"PeriodicalIF":2.6,"publicationDate":"2025-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143480975","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis, and neuroprotective activity of salidroside-based dual inhibitors of selective monoamine oxidase B and amyloid-β aggregation","authors":"Juan Zhang,&nbsp;Kong-Kai Zhu,&nbsp;Kai-Ming Wang,&nbsp;Cheng-Shi Jiang","doi":"10.1007/s00044-024-03367-0","DOIUrl":"10.1007/s00044-024-03367-0","url":null,"abstract":"<div><p>This study focuses on the design, synthesis, and evaluation of a series of salidroside derivatives (pOBZ-1~pOBZ-11) for their potential as inhibitors of monoamine oxidase B (MAO-B) and amyloid beta (Aβ₄₂) aggregation, and neuroprotective agents. Among the synthesized derivatives, pOBZ-1 and pOBZ-2 exhibited superior MAO-B inhibitory activity compared to salidroside, with notable selectivity over MAO-A. These compounds demonstrated linear competitive inhibition. Additionally, the derivatives effectively inhibited Aβ₄₂ aggregation and protected SH-SY5Y cells from Aβ₄₂ and hydrogen peroxide (H₂O₂)-induced neurotoxicity. The findings suggest that pOBZ-2, in particular, holds promise as a therapeutic candidate for Alzheimer’s disease.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div><div><p>Novel dual inhibitors of selective MAO-B/amyloid-β aggregation</p></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"625 - 637"},"PeriodicalIF":2.6,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143481007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis, and evaluation of benzylpiperidine-derived hydrazones as dual inhibitors of monoamine oxidases and acetylcholinesterase","authors":"Nikita Negi,&nbsp;Senthil R. Ayyannan,&nbsp;Rati K. P. Tripathi","doi":"10.1007/s00044-024-03365-2","DOIUrl":"10.1007/s00044-024-03365-2","url":null,"abstract":"<div><p>Alzheimer’s disease (AD) is a multifaceted neurodegenerative disorder characterized by cognitive decline and memory loss, with currently available treatments offering limited effectiveness, underscoring the need for multifunctional therapies. This study investigates benzylpiperidine derivatives as dual inhibitors of monoamine oxidases (MAOs) and acetylcholinesterase (AChE), enzymes implicated in AD pathology. Benzylpiperidine-derived hydrazones (4–13) were designed, synthesized and evaluated for inhibition against AChE and MAO-A/B isoforms. Among all, compounds <b>8</b> and <b>5</b> demonstrated a balanced multifunctional profile, effectively inhibiting MAO-A, MAO-B, and AChE. Compound <b>8</b> exhibited high potency against AChE (IC₅₀ = 0.064 ± 0.001 μM), comparable to donepezil (IC₅₀ = 0.084 ± 0.002 μM), with moderate inhibition of MAO-A (IC₅₀ = 2.55 ± 0.02 μM) and MAO-B (IC₅₀ = 1.47 ± 0.06 μM). Conversely, compound <b>5</b> displayed strongest inhibition against MAO-A (IC₅₀ = 0.26 ± 0.01 μM) and MAO-B (IC₅₀ = 0.116 ± 0.005 μM) within the series, along with moderate AChE inhibition (IC₅₀ = 3.70 ± 0.14 μM). Both compounds showed antioxidant activity, though mild neurotoxicity. Molecular docking studies highlighted crucial intermolecular interactions, including π-π stacking and H-bonding, essential for ligand-protein stabilization. Computational ADMET predictions suggested favorable drug-like properties, while conformational alignment studies further elucidated their binding efficiency compared to reference drugs. These findings showcase benzylpiperidine derivatives as potential multifunctional agents for further development in AD treatment, with compounds <b>8</b> and <b>5</b> emerging as primary leads for additional refinement.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"583 - 601"},"PeriodicalIF":2.6,"publicationDate":"2024-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143481108","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel alkoxy- and prenyl-xanthones derivatives as potential antidiabetic agents: Synthesis, in vitro evaluation and in silico studies","authors":"Gabriel Vázquez-Lira,&nbsp;Brandon Hernández-Gutierrez,&nbsp;María C. Cruz-López,&nbsp;Patricia Ibarra-Torres,&nbsp;Omar Gomez-García,&nbsp;Joaquín Tamariz,&nbsp;Aarón Mendieta-Moctezuma","doi":"10.1007/s00044-024-03364-3","DOIUrl":"10.1007/s00044-024-03364-3","url":null,"abstract":"<div><p>Novel alkoxy-xanthones <b>5</b>, <b>7</b>, <b>9</b>, <b>10</b>, and <b>10-14</b> were synthesized and evaluated in vitro for their ability to inhibit α-glucosidase, α-amylase, and pancreatic lipase. Compounds <b>5c</b>, <b>9</b> <b>d</b>, <b>11</b> <b>d</b>, and <b>14b</b> exhibited potent α-glucosidase inhibition (IC₅₀ 20.3, 32.4, 35.2, and 18.0 µM, respectively) while showing lower activity against α-amylase compared to acarbose (IC₅₀ 308.0 µM for α-glucosidase and 25.0 µM for α-amylase). In contrast, <b>9b</b> and <b>10c</b> demonstrated moderate inhibition and selectivity for α-amylase. Additionally, <b>10a</b> and <b>10c</b> displayed mild inhibitory effects across these digestive enzymes. These results suggest that the (4-chlorophenyl)-2-oxoethoxy moiety linked to the 3-hydroxy group of xanthone core is a potent inhibitor against of α-glucosidase and has mild activity against α-amylase, whereas the allyloxy moiety shows a modest inhibitory effect. Kinetic studies indicated that compounds <b>9b</b> and <b>11b</b> are mixed inhibitors of α-glucosidase and non-competitive inhibitors of α-amylase. For pancreatic lipase, <b>10c</b> acted as an uncompetitive inhibitor. Docking studies further supported the critical role of these hydrophobic groups in interacting with the catalytic pocket of these enzymes. ADMET studies identified derivatives <b>5c</b>, <b>10a</b>, <b>10c</b>, and <b>11b</b> as promising candidates for the developing antidiabetic agents.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"602 - 624"},"PeriodicalIF":2.6,"publicationDate":"2024-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143481109","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multivalent MMP-12 inhibitors as a valuable approach to counteract the intestinal epithelial barrier impairment and inflammation in an in vitro model mimicking intestinal high-fat exposure","authors":"Doretta Cuffaro,&nbsp;Vanessa D’Antongiovanni,&nbsp;Camilla Mangini,&nbsp;Clelia Di Salvo,&nbsp;Laura Benvenuti,&nbsp;Jennifer Vandooren,&nbsp;Marco Macchia,&nbsp;Luca Antonioli,&nbsp;Armando Rossello,&nbsp;Matteo Fornai,&nbsp;Elisa Nuti","doi":"10.1007/s00044-024-03361-6","DOIUrl":"10.1007/s00044-024-03361-6","url":null,"abstract":"<div><p>Intestinal epithelial barrier (IEB) impairment represents a prodromal event underlying obesity and related systemic inflammation. In this context, metalloproteinase-12 (MMP-12) has been reported to increase the IEB permeability through the reduction of tight junction proteins expression. Herein we report our effort to develop a small series of MMP-12 inhibitors as potential agents able to counteract the IEB alterations and intestinal inflammation associated with obesity. Three multivalent and gut-restricted carboxylate-based selective inhibitors of MMP-12 were synthesized and tested first on human recombinant MMP-12 isolated enzyme and then on human intestinal epithelial Caco-2 cells treated with palmitate (PA) and lipopolysaccharide (LPS), to mimic the in vivo exposure to hypercaloric diet. Trimeric derivative <b>2</b> in particular showed a nanomolar activity against MMP-12 and was able to increase both ZO-1 and claudin-1 tight junction expression in a concentration-dependent manner, already at a concentration of 50 nM. This compound was also the most effective in reducing interleukin-1β release from Caco-2 cells treated with PA and LPS. This preliminary work indicates that a pharmacological modulation of MMP-12 represents a promising strategy to counteract the impairment of IEB integrity and intestinal inflammation associated with obesity.</p></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 3","pages":"571 - 582"},"PeriodicalIF":2.6,"publicationDate":"2024-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143481107","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, bacteria activity and molecular simulation of D-galactose-conjugated thiosemicarbazones of 3-aryl-4-formylsydnones","authors":"Nguyen Dinh Thanh,&nbsp;Vu Ngoc Toan,&nbsp;Duong Ngoc Toan,&nbsp;Vu Minh Trang","doi":"10.1007/s00044-024-03363-4","DOIUrl":"10.1007/s00044-024-03363-4","url":null,"abstract":"<div><p>A series of D-galactose-conjugated substituted 4-formylsydnone thiosemicarbazones <b>4a-j</b> were designed and synthesized from appropriate substituted 3-aryl-4-formylsydnones <b>2a-j</b> and tetra-<i>O</i>-acetyl-β-<span>d</span>-galactopyranose <b>3</b>. These synthesized thioureas exhibited the remarkable inhibitory activity against both selected Gram-(+)- and Gram-(–)-bacteria. Amongst them, thiosemicarbazones <b>4a</b>,<b>b</b>,<b>c</b>,<b>f</b>,<b>j</b> were the most potent inhibitors against Gram-(+) bacterial strains with MIC values of 0.78–1.56 μg/mL, while compounds <b>4b</b>,<b>c</b>,<b>g</b>,<b>j</b> had the most inhibitions against Gram-(–) bacterial ones with MIC values of 0.78–1.56 μg/mL. The thiosemicarbazones <b>4b</b>, <b>4c</b>, <b>4</b> <b>f</b> and that contain simultaneously two methyl or methyl/nitro substituents on benzene ring exhibited the strong inhibition against both Gram-(+), including MRSA bacterium, and Gram-(–) bacterial strains with MIC values of 0.78–1.56 μg/mL. In addition, compound <b>4j</b> had strongest potent inhibitory activity against <i>S. aureus</i> DNA Gyrase and compound <b>4b</b> was the strongest inhibitor against <i>S. aureus</i> Topoisomerase IV. Almost all of the most potential compounds had low toxicity to WI-38 normal cell line. The in silico studies, including predictive ADMET and induced fit docking simulations, for the most potential compounds were performed. Molecular dynamics simulations applied for two most potential complexes <b>4b</b>/URN and <b>4j</b>/4URO to understand their mechanism of active interaction for these respective enzymes.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"34 2","pages":"476 - 495"},"PeriodicalIF":2.6,"publicationDate":"2024-12-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142925773","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, characterization, and evaluation of KDM4B inhibitors to attenuate inflammatory host immune response in periodontitis","authors":"Kathleen A. Garrabrant,&nbsp;Amelia B. Furbish,&nbsp;Jonathan M. Turner,&nbsp;Ivett Pina Gomez,&nbsp;Catherine M. Mills,&nbsp;Abhiram Maddi,&nbsp;Yuri K. Peterson","doi":"10.1007/s00044-024-03362-5","DOIUrl":"10.1007/s00044-024-03362-5","url":null,"abstract":"<div><p>Periodontal disease begins with bacterial plaque buildup in the oral cavity, inciting an inflammatory response that results in subsequent tissue damage. Even after standard treatment like scaling and root planning (SRP) to remove plaque and biofilm, the host immune response can remain hyper-active, perpetuating further tissue destruction. In these cases, aggressive periodontitis is resistant to SRP and the inflammatory response may persist, even in the absence of plaque, presenting a significant clinical challenge. Previous experiments have provided a validated model of periodontal inflammation by exposing murine macrophages to lipopolysaccharide (LPS) from <i>Aggregatibacter actinomycetemcomitans</i> (<i>Aa</i>), a pathogen linked to aggressive periodontitis. Using this model, we have previously demonstrated that the periodontal disease microenvironment triggers epigenetic changes, notably heightened lysine-specific demethylase 4B (KDM4B) activity. Data indicate that the KDM4B inhibitor ML324 can reverse the macrophage-mediated pro-inflammatory response induced by <i>Aa</i> LPS in vitro, providing compelling evidence for KDM4B as a rational therapeutic target for periodontal disease. In the present studies, a cohort of compounds was developed as potential KDM4B inhibitors. Synthesis and characterization of derivatives led to the discovery of compound <b>14</b> with an IC₅₀ of 170 nM against KDM4B and immunosuppressive activity in the <i>Aa</i> LPS challenge model. These results suggest KDM4B inhibitors as potential therapeutic agents for modulating the immune response for periodontal disease.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"33 12","pages":"2448 - 2462"},"PeriodicalIF":2.6,"publicationDate":"2024-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00044-024-03362-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142826435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CYP3A4 drug metabolism considerations in pediatric pharmacotherapy","authors":"Marin Vander Schaaf,&nbsp;Kyrle Luth,&nbsp;Danyelle M. Townsend,&nbsp;Katherine H. Chessman,&nbsp;Catherine M. Mills,&nbsp;Sandra S. Garner,&nbsp;Yuri K. Peterson","doi":"10.1007/s00044-024-03360-7","DOIUrl":"10.1007/s00044-024-03360-7","url":null,"abstract":"<div><p>Cytochrome P450 3A4 (CYP3A4) is a crucial enzyme involved in the Phase I metabolism of numerous medications used in clinical practice. Its potential significance in pediatric pharmacotherapy is underscored by the unique metabolic profile of children, which differs markedly from adults, especially in neonates, infants, and young children due to developmental changes in enzyme activity. This review explores the critical role of CYP3A4 in the metabolism of drugs used in the pediatric population, with a particular focus on combination drug therapies. Given the high potential for drug-drug interactions in combination therapies, understanding the modulation of CYP3A4 activity is essential for optimizing therapeutic outcomes and minimizing adverse effects. This paper further examines the structural similarities between these medications and bergamottin, a known CYP3A4 inhibitor found in citric fruits such as grapefruit. Variability in CYP3A4 activity, influenced by genetic polymorphisms, developmental stage, and external factors, necessitates careful consideration in the prescribing and management of drugs in children. This review corroborates the need for personalized medicine approaches and enhanced pharmacovigilance to ensure the safe and effective use of CYP3A4-metabolized drugs in the pediatric population.</p><h3>Graphical Abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"33 12","pages":"2221 - 2235"},"PeriodicalIF":2.6,"publicationDate":"2024-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00044-024-03360-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142826251","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In Memory of Professor Patrick M. Woster (1955–2023): a loss to the field of medicinal chemistry","authors":"David P. Rotella","doi":"10.1007/s00044-024-03359-0","DOIUrl":"10.1007/s00044-024-03359-0","url":null,"abstract":"","PeriodicalId":699,"journal":{"name":"Medicinal Chemistry Research","volume":"33 12","pages":"2181 - 2186"},"PeriodicalIF":2.6,"publicationDate":"2024-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142826331","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}