SARomics Biostructures AB

SARomics Biostructures provides key structures in drug design project

Pressmeddelande   •   Okt 20, 2010 12:32 CEST

Lund, Sweden, October 20, 2010 – SARomics Biostructures is pleased to announce the publication of its latest scientific results. The paper, which highlights the work of SARomics Biostructures and its co-founder Prof. Mikael Akke describes state-of-the-art investigations of the fundamental driving forces behind drug binding to proteins.

Diehl et al. (2010) “Conformational entropy and protein flexibility in ligand design targeting the carbohydrate recognition domain of galectin-3” J. Am. Chem. Soc. 132, 14577-14589, (Open access; freely available).

SARomics Biostructures provided crystallization and structure determination services within this exciting project. High-resolution protein structures are a prerequisite for detailed investigations of drug binding in molecular terms. In the present project, SARomics Biostructures determined the crystal structure of the carbohydrate recognition domain of galectin-3 in complex with a designed ligand at a resolution of 1.20 Å. The high-resolution structure made it possible for our clients to interpret experimental data from nuclear magnetic resonance relaxation and thereby explore the role of protein conformational entropy in modulating drug–target affinity.

The β-galactoside-binding protein galectin-3 is involved in the regulation of apoptosis, intracellular trafficking, cell signalling and cell adhesion. It is a potential target for treatments of cancer and inflammation.

About SARomics Biostructures

SARomics Biostructures AB is a privately held contract research organization specialized in structural biology services. The company accelerates its customers’ drug discovery processes by providing contract R&D support in the areas of protein crystallization, protein structure determination and NMR spectroscopy. Access to structural information increases molecular understanding and enables faster project execution.

SARomics Biostructures is equipped with state-of-the-art robotics for low volume high- throughput crystallization and X-ray diffraction experiments. Its location in close proximity to the MAX-lab synchrotron and its collaborative agreement with the synchrotron facility ensure rapid access to the beamlines, providing high quality synchrotron data and eliminating the need for costly and time consuming transportations of crystals to remote synchrotrons. In addition, its team is highly experienced in providing drug design services, which include computational chemistry, protein modelling and in silico protein optimization R&D support.

For more information, please visit