期刊
CHEMICAL BIOLOGY & DRUG DESIGN
卷 74, 期 5, 页码 457-467出版社
WILEY-BLACKWELL PUBLISHING, INC
DOI: 10.1111/j.1747-0285.2009.00889.x
关键词
CREDO; database; druggable; drugs; multi-protein complexes; PICCOLO; protein-protein interactions; small molecules; TIMBAL
资金
- UCB
- BBSRC
Growing evidence of the possibility of modulating protein-protein interactions with small molecules is opening the door to new approaches and concepts in drug discovery. In this paper, we describe the creation of TIMBAL, a hand-curated database holding an up to date collection of small molecules inhibiting multi-protein complexes. This database has been analysed and profiled in terms of molecular properties. Protein-protein modulators tend to be large lipophilic molecules with few hydrogen bond features. An analysis of TIMBAL's intersection with other structural databases, including CREDO (protein-small molecule from the PDB) and PICCOLO (protein-protein from the PDB) reveals that TIMBAL molecules tend to form mainly hydrophobic interactions with only a few hydrogen bonding contacts. With respect to potency, TIMBAL molecules are slightly less efficient than an average medicinal chemistry hit or lead. The database provides a resource that will allow further insights into the types of molecules favoured by protein interfaces and provide a background to continuing work in this area. Access at http://www-cryst.bioc.cam.ac.uk/timbal.
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