Isbn: 9786630056426 - in silico discovery of ndm-1 metallo-¿-lactamase inhibitors: against klebsiella pneumoniae a computational drug discovery approach (9 risultati)

PAP. Condizione: New. New Book. Shipped from UK. Established seller since 2000.

Condizione: New.

PAP. Condizione: New. New Book. Shipped from UK. Established seller since 2000.

Taschenbuch. Condizione: Neu. IN SILICO DISCOVERY OF NDM-1 METALLO-¿-LACTAMASE INHIBITORS | AGAINST KLEBSIELLA PNEUMONIAE A Computational Drug Discovery Approach | Raghavendra S | Taschenbuch | Englisch | 2026 | LAP LAMBERT Academic Publishing | EAN 9786630056426 | Verantwortliche Person für die EU: SIA OmniScriptum Publishing, Brivibas Gatve 197, 1039 RIGA, LETTLAND, customerservice[at]vdm-vsg[dot]de | Anbieter: preigu. …

Paperback. Condizione: new. Paperback. This book presents a comprehensive in silico drug discovery study focused on identifying potential inhibitors of New Delhi metallo-b-lactamase-1 (NDM-1), a key enzyme responsible for extensive b-lactam antibiotic resistance in Klebsiella pneumoniae. The work addresses the growing global threat of antimicrobial resistance and emphasizes the urgent need for novel therapeutic strategies against NDM-1-producing pathogens.The study follows a systematic computational workflow that includes protein retrieval and active-site identification, molecular docking, virtual screening, ADMET and toxicity prediction, and molecular dynamics (MD) simulations. The crystal structure of NDM-1 (PDB ID: 6NY7) was used as the target protein, and docking model validation was performed using the native ligand interactions.The findings conclude that the identified sulfonamide derivatives exhibit strong binding affinity, favorable ADME profiles, low toxicity, and stable interaction with NDM-1. The book establishes these compounds as potential lead candidates for further experimental validation and development against infections caused by NDM-1-producing Klebsiella pneumoniae. This item is printed on demand. Shipping may be from multiple locations in the US or from the UK, depending on stock availability.…

Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware 52 pp. Englisch.

Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - This book presents a comprehensive in silico drug discovery study focused on identifying potential inhibitors of New Delhi metallo-beta-lactamase-1 (NDM-1), a key enzyme responsible for extensive beta-lactam antibiotic resistance in Klebsiella pneumoniae. The work addresses the growing global threat of antimicrobial resistance and emphasizes the urgent need for novel therapeutic strategies against NDM-1-producing pathogens.The study follows a systematic computational workflow that includes protein retrieval and active-site identification, molecular docking, virtual screening, ADMET and toxicity prediction, and molecular dynamics (MD) simulations. The crystal structure of NDM-1 (PDB ID: 6NY7) was used as the target protein, and docking model validation was performed using the native ligand interactions.The findings conclude that the identified sulfonamide derivatives exhibit strong binding affinity, favorable ADME profiles, low toxicity, and stable interaction with NDM-1. The book establishes these compounds as potential lead candidates for further experimental validation and development against infections caused by NDM-1-producing Klebsiella pneumoniae.…

Paperback. Condizione: new. Paperback. This book presents a comprehensive in silico drug discovery study focused on identifying potential inhibitors of New Delhi metallo-b-lactamase-1 (NDM-1), a key enzyme responsible for extensive b-lactam antibiotic resistance in Klebsiella pneumoniae. The work addresses the growing global threat of antimicrobial resistance and emphasizes the urgent need for novel therapeutic strategies against NDM-1-producing pathogens.The study follows a systematic computational workflow that includes protein retrieval and active-site identification, molecular docking, virtual screening, ADMET and toxicity prediction, and molecular dynamics (MD) simulations. The crystal structure of NDM-1 (PDB ID: 6NY7) was used as the target protein, and docking model validation was performed using the native ligand interactions.The findings conclude that the identified sulfonamide derivatives exhibit strong binding affinity, favorable ADME profiles, low toxicity, and stable interaction with NDM-1. The book establishes these compounds as potential lead candidates for further experimental validation and development against infections caused by NDM-1-producing Klebsiella pneumoniae. This item is printed on demand. Shipping may be from our UK warehouse or from our Australian or US warehouses, depending on stock availability.…

Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware 52 pp. Englisch.