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ASINEX - Inspired by Nature BioFragments
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ASINEX's BioFragments
3500 compounds

Minimalist Molecules for Fragment-based Lead Discovery

ASINEX is constantly improving the design of small molecule screening compounds to address the needs of modern drug discovery technologies. Fragment-based drug design is now a well-established technique which has been incorporated into the lead-seeking efforts of many research groups in academia and industry.

ASINEX has focused on the design and synthesis of novel fragment-like molecules (MW < 300) that contain a high density of minimalist pharmacophore elements and which are associated with increased protein binding properties [1]. Special attention was paid to conformationally constrained sp3-rich molecules with sophisticated 3D architecture and possessing multiple stereogenic centers. These properties are inherent to structurally more complex and diverse natural products, while traditional commercial fragment libraries are usually excessively populated with aromatic, flat and achiral compounds.


ASINEX's BioFragments do not contain undesirable functionalities and have been optimized in terms of physico-chemical parameters. All compounds have been developed towards and tested for solubility in aqueous and DMSO media at high concentrations. Since all compounds have exceptionally good DMSO and PBS solubility, they are compatible with all types of biochemical and biophysical assays. Moreover the BioFragment library is supported by complimentary sets of precursors and elaborated analogues to facilitate further fragment-to-lead optimization activities.


Library specifics
Size: 3500 compounds
Structure identity confirmed by NMR, X-ray crystallography
Measured Solubility: 100% of compounds are soluble in DMSO at 10 mM, and in PBS at 100 µM
Quality: min.purity of 95% (LC-MS, NMR), stored as dry powder

ASINEX's BioFragments is only available upon request, please contact us at:
Tel.: +7 (495) 780 34 10, +7 (495) 780 34 15
E-mail : or

1. Paul A. Clemons et al., Small molecules of different origins have distinct distributions of structural complexity that correlate with protein-binding profiles, PNAS November 2, 2010 vol. 107 no. 44 18787-18792



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