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Current Medicinal Chemistry is a peer-reviewed medical journal published by Bentham Science Publishers. The editor-in-chief is Atta-ur-Rahman, FRS (Kings College University of Cambridge Cambridge, UK). The journal covers developments in medicinal chemistry and rational drug design and publishes original research reports and review papers. [2]
Current Medicinal Chemistry; Current Molecular Medicine; Current Molecular Pharmacology; Current Nanoscience; Current Neuropharmacology; Current Neurovascular Research; Current Nutrition & Food Science; Current Organic Chemistry; Current Organic Synthesis; Current Pediatric Reviews; Current Pharmaceutical Analysis; Current Pharmaceutical ...
Current Topics in Medicinal Chemistry is a biweekly peer-reviewed medical journal published by Bentham Science Publishers. It includes review articles on all aspects of medicinal chemistry, including drug design. The current editor-in-chief is Jia Zhou (University of Texas, Medical Branch).
Description: An encyclopedic text and reference suitable for advanced undergraduate or graduate study. Importance: This massive text by outstanding research workers begins with simple systems and proceeds logically to the more complex phenomena of physical chemistry. The original literature is cited extensively, making the work useful as a ...
The phrase "drug design" is similar to ligand design (i.e., design of a molecule that will bind tightly to its target). [6] Although design techniques for prediction of binding affinity are reasonably successful, there are many other properties, such as bioavailability, metabolic half-life, and side effects, that first must be optimized before a ligand can become a safe and effictive drug.
Medicinal or pharmaceutical chemistry is a scientific discipline at the intersection of chemistry and pharmacy involved with designing and developing pharmaceutical drugs. Medicinal chemistry involves the identification, synthesis and development of new chemical entities suitable for therapeutic use.
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The mechanism of the HIV protease shares many features with the rest of the aspartic protease family although the full detailed mechanism of this enzyme is not fully understood. [12] The water molecule seems to play a role in the opening and closing of the flaps as well as increasing the affinity between enzyme and substrate.
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