Chemical Biology & Drug Design
© John Wiley & Sons A/S. Published by John Wiley & Sons Ltd
Edited By: David Selwood
Impact Factor: 2.469
ISI Journal Citation Reports © Ranking: 2012: 27/59 (Chemistry Medicinal); 176/290 (Biochemistry & Molecular Biology)
Online ISSN: 1747-0285
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Reasons to publish with CB & DD
• Rapid review and publishing: 30 days on average from submission to first decision. We discourage reviewers from requesting “additional experiments”.
• Simple initial submission process, can load a single PDF.
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BIT's 11th Annual Congress of International Drug Discovery Science & Technology, Therapy and EXPO
The 11th Congress of International Drug Discovery Science and Technology 2013 aims to offer professionals in the field of drug discovery a multidisciplinary platform to discuss and to share knowledge about the latest scientific discoveries and current industry standards. The IDDST is also the place to start interesting new collaborations between academia, industry and institutes to further develop or apply drug discovery and technologies towards the market.
Recently Published Articles
- Comparison of binding characterization of two antiviral drugs to Human Serum Albumin
M Li, E McAuley, Y Zhang, LL Kong, F Yang, ZP Zhou, XY Wu and H Liang
Accepted manuscript online: 10 DEC 2013 11:02AM EST | DOI: 10.1111/cbdd.12270
The model on the interactions of antiviral drugs with HSA was built by fluorescence spectroscopy and X-ray crystallography; the binding mechanism and behaviour of antiviral drugs to HSA were determined and compared ;the interactive associations of drug-drug binding with IIA subdomain of HSA was studied. The results provided guidence for future development of ribovirin and lamivudine based compounds and a drug-HSA delivery system.
- Preparation, optimization and characterization of bovine lactoferrin loaded liposomes and solid lipid particles modified by hydrophilic polymers using factorial design
Xudong Yao, Craig Bunt, Jillian Cornish, Siew-Young Quek and Jingyuan Wen
Accepted manuscript online: 10 DEC 2013 11:02AM EST | DOI: 10.1111/cbdd.12269
Lactoferrin is an ideal candidate for incorporation into a controlled release formulation due to it's poor oral bioavailability. In presence of pectin or chitosan, lactoferrin loaded particles formed net like structures consisting of polymeric network in which multiple particles were imbedded. Lactoferrin encapsulated in pectin and chitosan modified liposomes and solid lipid particles showed prolong mean residence time in rat blood and increased the relative bioavailability compared with free drug.
- Novel Central Nervous System Drug Delivery Systems
Jocelyn Stockwell, Nabiha Abdi, Xiaofan Lu, Oshin Maheshwari and Changiz Taghibiglou
Accepted manuscript online: 10 DEC 2013 11:02AM EST | DOI: 10.1111/cbdd.12268
Novel systems of drug delivery to the central nervous system are reviewed. Multiple methods, including invasive and non-invasive methods are examined.
- Benzocaine complexation with p-sulfonic acid calix[n]arene: experimental (1H-NMR) and theoretical approaches
Lucas Micquéias Arantes, Eduardo Vinícius Vieira Varejão, Karin Juliane Pelizzaro-Rocha, Cíntia Maria Saia Cereda, Eneida de Paula, Maicon Pierre Lourenço, Hélio Anderson Duarte and Sergio Antonio Fernandes
Accepted manuscript online: 2 DEC 2013 01:14AM EST | DOI: 10.1111/cbdd.12267
The architetures of inclusion complexes between benzocaine and p-sulfonic acid calix[n]arenes were characterized by means of experimental 1H NMR spectroscopy and theoretical calculations. In vitro cytotoxic tests showed that complexation intensifies the intrinsic toxicity of benzocaine, possibly by favoring its partitioning inside biomembranes.
- Structure-Based Evaluation of C5 Derivatives in the Catechol Diether Series Targeting HIV-1 Reverse Transcriptase
Kathleen M. Frey, William T. Gray, Krasimir A. Spasov, Mariela Bollini, Ricardo Gallardo-Macias, William L. Jorgensen and Karen S. Anderson
Accepted manuscript online: 2 DEC 2013 01:14AM EST | DOI: 10.1111/cbdd.12266
Potent inhibitors of HIV-1 targeting reverse transcriptase are evaluated using x-ray crystallography to elucidate the molecular interactions in the non-nucleoside binding pocket. Comparison of four crystal structures reveals unique binding modes of the inhibitors that correlate well with their respective potencies. An interaction between conserved residue Pro95 and the 5-Cl of the leading inhibitor may influence an optimal conformation for binding in the pocket and may be further exploited for future optimization of the compound series.