More and more companies are using fragment-based lead design as a drug discovery strategy » All About Drugs

More and more companies are using fragment-based lead design as a drug discovery strategy » All About Drugs:



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Antimalarials………….Arterolane from Ranbaxy « New Drug Approvals

Antimalarials………….Arterolane from Ranbaxy « New Drug Approvals:



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Evacetrapib, LY2484595 for Treatment of high cholesterol and preventing cardiac events « New Drug Approvals

Evacetrapib, LY2484595 for Treatment of high cholesterol and preventing cardiac events « New Drug Approvals:



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Novel Oxazolidinone Antibacterial Candidate FYL-67 …..(S)-N-((3-(3-Fluoro-4-(4-(pyridin-2-yl)-1H-pyrazol-1-yl)phenyl)-2-oxo-oxazolidin-5-yl)methyl)acetamide « New Drug Approvals

Novel Oxazolidinone Antibacterial Candidate FYL-67 …..(S)-N-((3-(3-Fluoro-4-(4-(pyridin-2-yl)-1H-pyrazol-1-yl)phenyl)-2-oxo-oxazolidin-5-yl)methyl)acetamide « New Drug Approvals:



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A novel approach to identify molecular binding to the influenza virus H5N1: screening using molecularly imprinted polymers (MIPs)

http://pubs.rsc.org/en/Content/ArticleLanding/2014/MD/C3MD00272A?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+rss%2FMD+%28RSC+-+Med.+Chem.+Commun.+latest+articles%29#!divAbstract

In this report we investigate whether a molecularly imprinted polymer (MIP) of an inactivated strain of influenza A H5N1 could be used to help identify molecules capable of binding to, and inhibiting the function of the virus, via either competitive or allosteric mechanisms. Molecules which bind to the virus and induce a conformational change are expected to show reduced binding to the H5N1 specific MIP. Given the importance of molecular recognition in virus replication, such conformational change might also reduce the effectiveness of neuraminidase (N1) for cleaving the sialic groups necessary for virus replication. We show that the method can indeed differentiate between a potent neuraminidase inhibitor, H1 and H5 antibodies, and N1 specific and non-specific monosaccharide substrates. We suggest that such a method could potentially be used in conjunction with traditional biochemical assays to facilitate the identification of molecules functioning via novel modes of action.

Med. Chem. Commun., 2014, Advance Article
DOI: 10.1039/C3MD00272A, Concise Article

Thipvaree Wangchareansak, Arunee Thitithanyanont, Daungmanee Chuakheaw, M. Paul Gleeson, Peter A. Lieberzeit, Chak Sangma
We investigate whether a molecularly imprinted polymer (MIP) of influenza A H5N1 could be used to help identify molecules capable of binding to, and inhibiting the function of the virus, via either competitive or allosteric mechanisms.

A novel approach to identify molecular binding to the influenza virus H5N1: screening using molecularly imprinted polymers (MIPs)

OMARIGLIPTIN. MK 3102 IN PHASE 3 FOR TYPE 2 DIABETES « New Drug Approvals

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Carbohydrate Derivatives and Glycomimetic Compounds in Established and Investigational Therapies of Type 2 Diabetes Mellitus « New Drug Approvals

Carbohydrate Derivatives and Glycomimetic Compounds in Established and Investigational Therapies of Type 2 Diabetes Mellitus « New Drug Approvals:



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