X-ray Crystallography Services
FastLane™ Structures, Gene-to-Structure & Protein-Ligand co-Crystallization
Our X-ray crystallography services platform handles, on average, over 100 projects annually. Through our work with nearly all large pharmaceutical companies, more than 100 biotech companies, and academic groups, we have gathered extensive experience in all areas of structural biology, including all types of crystallization and X-ray crystallographic problems (more than 500 disclosable X-ray and NMR spectroscopy structures have been deposited to the PDB). Moreover, thanks to the high professional level of our employees and the optimization of our work process, we can provide highly competitive prices! Our publications provide many examples of our contributions.
Please see below for the details of our libraries of drug-target structures and gene-to-structure services. In addition, our structural biology platform overview provides details of our X-ray crystallography services.
Please see below for the details of our libraries of drug-target structures and gene-to-structure services. In addition, our structural biology platform overview provides details of our X-ray crystallography services.
You may also search here for the protein of interest:
Library of verified drug targets that have already been expressed, purified, and crystallized at the company (off-the-shelf structures). Purified proteins are available for the immediate start of a project.
Library of verified drug targets for which expression plasmids and protocols for expression, purification, and crystallization are available at the company.
Gene-to-structure services include cloning, expression, purification, characterization, crystallization, and high resolution X-ray structure determination.
Several proteins from the FastLane™ Premium library can also be purchased for scientific use. Please view our catalog of high-purity crystallization-grade recombinant proteins.
FastLane™ Premium library
The FastLane™ Premium library currently contains drug target proteins ready for co-crystallization with ligands. The library includes an extensive collection of kinases, phosphatases, proteases, epigenetic factors, and other drug targets. Using our high-throughput X-ray crystallography pipeline, the turnaround time for structure determination for these proteins is between 2 to 8 weeks (depending on the protein).
- Kinases
Gene Protein BTK Tyrosine-protein kinase BTK CDK2 Cyclin-dependent kinase 2 CDK5 Cyclin-dependent-like kinase 5 CK2 Casein kinase II subunit alpha CLK3 Dual specificity protein kinase CLK3 DAPK3 Death-associated protein kinase 3 DYRK1A Dual specificity tyrosine-phosphorylation-regulated kinase 1A EPHA7 Ephrin type-A receptor 7 ERBB2 HER2, Receptor tyrosine-protein kinase erbB-2, extracellular domain FGFR1 Fibroblast growth factor receptor 1 LATS2 Serine/threonine-protein kinase LATS2 MAP2K4 Dual specificity mitogen-activated protein kinase kinase 4 PFKFB3 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 PIM1 Serine/threonine-protein kinase pim-1 PIM3 Serine/threonine-protein kinase pim-3 PIP4K2A Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha PLK4 Serine/threonine-protein kinase PLK4 RSK1 RPS6KA1 Ribosomal protein S6 kinase alpha-1 STK10 LOK or Serine/threonine-protein kinase 10 STK17A DRAK1 or Serine/threonine-protein kinase 17A STK17B DRAK2 or Serine/threonine-protein kinase 17B Vps34 PIK3C3 Phosphatidylinositol 3-kinase catalytic subunit type 3 - Epigenetic targets
- Proteases & phosphatases
Gene Protein DPP4 Dipeptidyl peptidase 4 Thrombin F2, Human alpha thrombin PTPN1 PTP1B, Tyrosine-protein phosphatase non-receptor type 1 SHP2 PTPN11, Tyrosine-protein phosphatase non-receptor type 11 USP21 UBP21, Ubiquitin carboxyl-terminal hydrolase 21 USP7 UBP7, Ubiquitin carboxyl-terminal hydrolase 7 USP8 UBP8, Ubiquitin carboxyl-terminal hydrolase 8 - Other targets
Gene Protein Aldose reductase ALDR, Aldose reductase BCAT2 Branched-chain-amino-acid aminotransferase, mitochondrial BCL2A1 BFL1, Bcl-2-related protein A1 BSSL Bile salt-activated lipase CathepsinC CPPI, Dipeptidyl peptidase 1 CD137 TNFRSF9, Tumor necrosis factor receptor superfamily member 9 CD47 Leukocyte surface antigen CD47 CGAS Cyclic GMP-AMP synthase CYP51A1 Lanosterol 14-alpha demethylase DHODH Dihydroorotate dehydrogenase EIF4E Eukaryotic translation initiation factor 4E Gal-3C LGALS3, Galectin-3 C-terminal carbohydrate binding domain Gal-8N LGALS8, Galectin 8 N-terminal carbohydrate binding domain GART Trifunctional purine biosynthetic protein adenosine-3 GMPR2 GMP reductase 2 GP6 Platelet glycoprotein VI HSP90AA1 Heat shock protein HSP 90-alpha IL17A IL-17A, Interleukin-17A IL23A IL-23A, Interleukin-23, subunits alpha and beta CXCL8 IL-8, Interleukin-8 LDHA LDHA, L-lactate dehydrogenase A chain (rabbit) NRP1 Neuropilin-1 PDE4D cAMP-specific 3',5'-cyclic phosphodiesterase 4D PSD95 DLG4, Disks large homolog 4 RORC Nuclear receptor ROR-gamma S100A12 Protein S100-A12 S100A4 Mts1 or Protein S100-A4 S100A9t MRP14, Protein S100-A9 TIM-3 HAVCR2 , Hepatitis A virus cellular receptor 2 F3 TF, Tissue factor TNF-alpha Tumor necrosis factor TUBA1A Tubulin alpha-1A (pig) UBA52 Ubiquitin-60S ribosomal protein L40 - Non-human proteins
Gene Protein blaC Beta-lactamase (M. tuberculosis) gyrB DNA gyrase subunit B (S. aureus) Snf LeuT, Na(+):neurotransmitter symporter, Snf family (Aquifex aeolicus VF5) SARS CoV-2 RBD Spike glycoprotein receptor-binding domain (SARS-CoV-2) SARS CoV-2 RBD beta Spike glycoprotein receptor-binding domain, B.1.351 variant (SARS-CoV-2)
On the image: Björn Walse, PhD, CEO SARomics Biostructures, and Raymond Kimbung, PhD, Senior Scientist, Team Leader, Protein Production
FastLane™ Standard library
The FastLane™ Standard library currently contains more than 150 constructs of drug target proteins ready for expression, purification, crystallization, and X-ray structure determination according to verified protocols. The library includes a large number of protein kinases, phosphatases, epigenetic factors, and other drug targets. Using our high-throughput X-ray crystallography pipeline, the turnaround time for structure determination for these proteins is between 6 to 12 weeks (depending on the protein).
Please click to view the available FastLane™ Standard proteins
- Kinases AK1 - Adenylate kinase isoenzyme 1 (a.a. 1-193).
AK2 - Adenylate kinase isoenzyme 2, mitochondrial (a.a. 1-239).
AK3L1 - Adenylate kinase isoenzyme 4, mitochondrial (a.a. 1-223).
AK5 - Adenylate kinase isoenzyme 5 (a.a. 366-562).
BMPR2 - Bone morphogenetic protein receptor type-2 (a.a. 189-517).
CAMK1D - Calcium/calmodulin-dependent protein kinase type 1D (a.a. 1-333).
CAMK1G - Calcium/calmodulin-dependent protein kinase type 1G (a.a. 18-316).
CAMK2A - Calcium/calmodulin-dependent protein kinase type II subunit alpha (a.a. 13-302).
CAMK2B - Calcium/calmodulin-dependent protein kinase type II subunit beta (a.a. 11-303).
CAMK2D - Calcium/calmodulin-dependent protein kinase type II subunit delta (a.a. 11-309).
CAMK2G - Calcium/calmodulin-dependent protein kinase type II subunit gamma (a.a. 5-315).
CAMK4 - Calcium/calmodulin-dependent protein kinase type IV (a.a. 15-340).
CLK1 - Dual specificity protein kinase CLK1 (a.a. 148-484).
CLK2 - Dual specificity protein kinase CLK2 (a.a. 135-496).
CLK3 - Dual specificity protein kinase CLK3 (a.a. 284-638).CSNK1G1 - Casein kinase I isoform gamma-1 (a.a. 45-352).
CSNK1G2 - Casein kinase I isoform gamma-2 (a.a. 43-353).
CSNK1G3 - Casein kinase I isoform gamma-3 (a.a. 35-362).
DMPK - Myotonin-protein kinase (a.a. 11-420).
DYRK2 - Dual specificity tyrosine-phosphorylation-regulated kinase 2 (a.a. 146-552).
FLT1 (VEGFR1) - Tyrosine-protein kinase receptor FLT (a.a. 801-1158).
GAK - Cyclin-G-associated kinase (a.a. 12-347).
HASPIN - GSG2 or Serine/threonine-protein kinase haspin (a.a. 465-798).
ITPK1 - Inositol-tetrakisphosphate 1-kinase (a.a. 1-327).
ITPKC - Inositol-trisphosphate 3-kinase C (a.a. 425-683).
MAP2K6 - Dual specificity mitogen-activated protein kinase kinase 6 (a.a. 47-334)
MAP3K5 - Mitogen-activated protein kinase kinase kinase 5 (MAPK/ERK kinase kinase 5), (a.a. 659-951).
MAPK11 - Mitogen-activated protein kinase 11 (p38b), (a.a. 5-350).
MAPK6 - Mitogen-activated protein kinase 6 (a.a. 9-327).
MPSK1 - STK16 or Serine/threonine-protein kinase 16 (a.a. 13-305).
MST4 - STK26, Serine/threonine-protein kinase (a.a. 1-300).NEK2 - Serine/threonine-protein kinase (a.a. 1-271).
PAK4 - Serine/threonine-protein kinase PAK 4 (a.a. 291-591).
PAK5 - Serine/threonine-protein kinase PAK 5 (a.a. 425-719).
PAK6 - Serine/threonine-protein kinase PAK 6 (a.a. 383-681).
PCTK1 - CDK16, Cyclin-dependent kinase 16 (a.a. 163-478).
PHKG2 - Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (a.a. 6-293).
PIP5K2C - PIP4K2C, Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (a.a. 32-421).
PKM - PKM2, Pyruvate kinase isozymes (a.a. 3-530).
PTK2B - Protein-tyrosine kinase 2-beta (a.a. 414-692).
SLK - STE20-like serine/threonine-protein kinase (a.a. 19-320).
SRPK2 - SRSF protein kinase 2 (a.a. 51-688).
TTK - MPS1, Dual specificity protein kinase TTK (a.a. 519-808).
VRK1 - Serine/threonine-protein kinase (a.a. 3-364).
VRK2 - Serine/threonine-protein kinase (a.a. 14-335).
VRK3 - Inactive serine/threonine-protein kinase VRK3 (a.a. 146-474).
YSK1 - STK25, Serine/threonine kinase 25 (a.a. 1-293). - Phosphatases DUSP13 - Dual specificity protein phosphatase 13 isoform B (a.a. 1-198).
IMPA2 - Inositol monophosphatase 2 (a.a. 16-288).
INPP5B - Type II inositol 1,4,5-trisphosphate 5-phosphatase (a.a. 339-643)
INPP5E - 72 kDa inositol polyphosphate 5-phosphatase (a.a. 275-623).
INPPL1 - Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (a.a. 419-732).
ITPA - Inosine triphosphate pyrophosphatase (a.a. 1-194).
LHPP - Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (a.a. 1-270).
MDP1 - Magnesium-dependent phosphatase 1 (a.a. 1-165).
MTMR6 - Myotubularin-related protein 6 (a.a. 1-505).
NANP - N-acylneuraminate-9-phosphatase (a.a. 1-248).PHPT1 - 14 kDa phosphohistidine phosphatase (a.a. 5-125).
PTPN3 - Non-receptor tyrosine-protein phosphatase type 3 (a.a. 628-913).
PTPN4 - Non-receptor tyrosine-protein phosphatase type 4 (a.a. 611-926).
PTPN5 - Non-receptor tyrosine-protein phosphatase type 5 (a.a. 282-563).
PTPN7 - Non-receptor tyrosine-protein phosphatase type 7 (a.a. 65-358).
PTPN9 (MEG2) - Non-receptor tyrosine-protein phosphatase type 9 (a.a. 277-582).
PTPN14 - Non-receptor tyrosine-protein phosphatase type 14 (a.a. 886-1187)
PTPN18 - Non-receptor tyrosine-protein phosphatase type 18 (a.a. 6-299).
PTPN22 - Non-receptor tyrosine-protein phosphatase type 22 (a.a. 1-302).
PTPRB - Receptor-type tyrosine-protein phosphatase beta (a.a. 1686-1971).PTPRE - Receptor-type tyrosine-protein phosphatase epsilon (a.a. 107-697).
PTPRG - Receptor-type tyrosine-protein phosphatase epsilon (a.a. 827-1445).
PTPRJ - Receptor-type tyrosine-protein phosphatase eta (a.a. 1019-1311).
PTPRK - Receptor-type tyrosine-protein phosphatase eta (a.a. 865-1154).
PTPRN2 - Receptor-type tyrosine-protein phosphatase N2 (a.a. 715-1010).
PTPRO - Receptor-type tyrosine-protein phosphatase O (a.a. 916-1208).
PTPRR - Receptor-type tyrosine-protein phosphatase R (a.a. 375-655).
PTPRT - Receptor-type tyrosine-protein phosphatase T (a.a. 868-1151).
RNGTT - mRNA-capping enzyme (a.a. 1-219).
THTPA - Thiamine-triphosphatase (a.a. 1-215). - Epigenetic targets: Bromodomains ASH1L - Bromodomain, Histone-lysine N-methyltransferase ASH1L (a.a. 2438-2561).
BAZ2B - Bromodomain adjacent to zinc finger domain protein 2B (a.a. 2054-2168).
BPTF - Bromodomain, Nucleosome-remodeling factor subunit BPTF (a.a. 2914-3037).
BRD1 - Bromodomain-containing protein 1 (a.a. 556-688).
BRD9 - Bromodomain-containing protein 9 (a.a. 134-239).
BRWD1 - Bromodomain and WD repeat-containing protein 1 (a.a. 1310-1430 Bromodomain 2).
CECR2 - Bromodomain, Cat eye syndrome critical region protein 2 (a.a. 424-538).CREBBP - Bromodomain, CREB-binding protein (a.a. 1081-1197).
EP300 - Bromodomain, Histone acetyltransferase p300, (a.a. 1040-1161).
KAT2A - Bromodomain, Histone acetyltransferase KAT2A, (a.a. 729-837).
KAT2B - Bromodomain, Histone acetyltransferase KAT2B (a.a. 715-831).
PBRM1 - Bromodomain, Protein polybromo-1 (a.a. 43-156).
PBRM1 - Bromodomain, Protein polybromo-1 (a.a. 178-291).
PBRM1 - Bromodomain, Protein polybromo-1 (a.a. 388-494).
PBRM1 - Bromodomain, Protein polybromo-1 (a.a. 645-766).PBRM1 - Bromodomain, Protein polybromo-1 (a.a. 773-917).
PHIP - Bromodomain, PH-interacting protein (a.a. 1302-1434).
TAF1 - Bromodomain, Transcription initiation factor TFIID subunit 1 (a.a. 1373-1635, Bromodomains 1 & 2).
TAF1 - Bromodomain, Transcription initiation factor TFIID subunit 1 (a.a. 1501-1635 Bromodomain 2).
TAF1L - Bromodomain, Transcription initiation factor TFIID subunit 1-like (a.a. 1523-1654). - Epigenetic targets: Demethylases & others JMJD2A - Lysine-specific demethylase 4A (a.a. 1-359).
JMJD2B - KDM4B or Lysine-specific demethylase 4B (a.a. 1-346).
JMJD2C - KDM4C or Lysine-specific demethylase 4C (a.a. 875-995 tudor domains).
JMJD2D - KDM4D or Lysine-specific demethylase 4C (a.a. 12-341).
JMJD3 - Lysine-specific demethylase 6B (a.a.1176-1502).
JMJD6 - Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (a.a. 1-335).KDM4E - KDM4DL or Lysine-specific demethylase 4E (a.a. 1-336).
MINA - Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA (a.a. 26-465).
PHF8 - Histone lysine demethylase PHF8 (a.a. 115-483).
PARP2 - Poly [ADP-ribose] polymerase 2 (a.a. 235-579).
PARP3 - Poly [ADP-ribose] polymerase 3 (a.a. 178-532).
PARP10 - Poly [ADP-ribose] polymerase 10 (a.a. 09-1017).PARP12 - Poly [ADP-ribose] polymerase 12(a.a. 89-684).
PARP14 - Poly [ADP-ribose] polymerase 14(a.a. 1611-1801).
PARP15 - Poly [ADP-ribose] polymerase 15 (a.a. 459-656).
TNKS - Tankyrase-1 (a.a. 1091-1325).
TNKS2 - Tankyrase-2 (a.a. 946-1152).
ZC3HAV1 - Zinc finger CCCH-type antiviral protein 1 (a.a. 724-896). - Others ARNT - Aryl hydrocarbon receptor nuclear translocator (a.a. 356-470).
BAK1 - Bcl-2 homologous antagonist/killer, mitochondrial apoptosis regulator (a.a. 21-190).
BCL2A1 - Bcl-2-related protein A1 (a.a. 1-149).
DPP4 - Dipeptidyl peptidase 4.
EPAS1 - Hif2a or Endothelial PAS domain-containing protein 1 (a.a. 239-350).
GLS - Glutaminase kidney isoform, mitochondrial (a.a. 221-533).
GMPR2 - GMP reductase 2 (a.a. 10-341).
MTH1 - NUDT1 or 7,8-dihydro-8-oxoguanine triphosphatase (a.a. 42-197).
NT5C2 - Cytosolic purine 5'-nucleotidase (a.a. 1-536).
NT5C3 - Cytosolic 5'-nucleotidase 3A (a.a. 64-336).
NUDT3 - Diphosphoinositol polyphosphate phosphohydrolase 1 (a.a. 1-172).
NUDT6 - Nucleoside diphosphate-linked moiety X motif 6 (a.a. 141-316).
NUDT10 - Diphosphoinositol polyphosphate phosphohydrolase 3-alpha (a.a. 17-144).NUDT14 - Uridine diphosphate glucose pyrophosphatase (a.a. 28-222).
NUDT16 - U8 snoRNA-decapping enzyme (a.a. aa1-aa195).
NUDT16L1 - Protein syndesmos (a.a.6-211).
NUDT18 - 8-oxo-dGDP phosphatase NUDT18 (a.a. 26-179).
NUDT21 - Cleavage and polyadenylation specificity factor subunit 5 (a.a.21-227).
PHGDH - D-3-phosphoglycerate dehydrogenase (a.a 4-314).
PSAT1 - Phosphoserine aminotransferase (a.a. 17-370).
PPARG - Peroxisome proliferator-activated receptor gamma (a.a. 232-505).
PYCR1 - Pyrroline-5-carboxylate reductase 1, mitochondrial (a.a. 1-300).
ROR-gamma - Nuclear receptor ROR-gamma.
THEM2 - Acyl-coenzyme A thioesterase 13 (a.a. 19-140).
USP2 - Ubiquitin carboxyl-terminal hydrolase 2 (a.a. 258-605).
USP5 - Ubiquitin carboxyl-terminal hydrolase 5 (a.a. 163-291).
Gene to structure services
SARomics Biostructures' X-ray crystallography services platform also provides gene-to-structure services, which include cloning, expression, purification of proteins, and characterization using biophysical methods, followed by crystallization, X-ray data collection either at the MAX IV synchrotron in Lund or at some other European synchrotron, followed by high resolution structure analysis. For optimal handling, high-throughput protein characterization and crystallization protocols have been developed at the company and used throughout the process.
Gene-to-Structure services are performed on a fee-for-service basis and include:
More details on the methods used in X-ray crystallography services can be found on our Learning Center protein crystallization page. Contact us directly to discuss your project using the contact form.
Gene-to-Structure services are performed on a fee-for-service basis and include:
- Cloning, expression, and purification of the protein
- Biophysical characterization using dynamic light scattering (DLS), CD spectroscopy, differential scanning fluorimetry (DSF), and, if appropriate, NMR spectroscopy.
- Crystallization, X-ray data collection, and structure determination.
- Protein-ligand co-crystallization and structure determination.
More details on the methods used in X-ray crystallography services can be found on our Learning Center protein crystallization page. Contact us directly to discuss your project using the contact form.
Maria Håkansson, PhD, Principal Scientist, Team Leader, Protein Crystallography, and Raymond Kimbung, PhD, Senior Scientist, Team Leader, Protein Production
Crystallography services outline: Cloning, expression, purification and characterization
Obtaining well-diffracting crystals is an art. To accelerate the process, we have developed proprietary protocols for the optimal handling of all project steps. The first step is defining the correct protein construct, followed by cloning, expression, and purification. Construct definition is essential since, in many examples removing just a couple of amino acid residues, e.g., at the N-terminus, dramatically improved protein crystal quality and the quality of the X-ray data. Among other methods, NMR spectroscopy can verify if the construct yields a folded, well-behaved protein. In addition, other biophysical methods like Dynamic Light Scattering (DLS), CD spectroscopy, and Differential Scanning Fluorimetry (DSF, also called thermal shift assay) may be used for verification. Obtaining a monodisperse solution of the protein is essential for successful crystallization. For illustration, a product sheet that shows the characteristics of a crystallization-grade protein from our Protein Shop can be downloaded here.
A plate hotel is used for storing and monitoring crystallization plates, usually kept at a constant temperature.
The 96-well crystallization plate from Hampton Research.
The 96-well crystallization plate from Hampton Research.
Crystallization & synchrotron X-ray data collection
X-ray protein crystallography is central to structural biology. And protein crystallography requires crystals! If crystallization conditions are unknown, we use our commercial and proprietary screens collection to identify initial crystallization conditions. Crystallization robotics is used in this process, while the crystallization plates are kept in plate hotels at a constant temperature. The plates are periodically monitored using an automated imaging system. Usually, the initial conditions need to be optimized to obtain well-diffracting crystals. The crystals are tested using synchrotron radiation. On average, we collect X-ray data on European synchrotrons every second week, on-site or remotely. Lund's MAX IV synchrotron radiation facility is just a few kilometers from our lab. Please see our technology pages for additional details on our protein X-ray crystallography services.
X-ray structure determination
Model building and refinement can start after collecting good-quality X-ray data and obtaining an electron density map. At this stage, the presence of a ligand (in the case of a protein-ligand complex) can quickly be assessed. Our customers are periodically informed of the project's progress, and any deviations from the plan are discussed before proceeding.
More details on sample preparation can be found in our guidelines for preparing and sending samples for crystallization.
Please do not hesitate to contact us if you require assistance preparing samples or any other information.
More details on sample preparation can be found in our guidelines for preparing and sending samples for crystallization.
Please do not hesitate to contact us if you require assistance preparing samples or any other information.
Antibody structure
Structure-based drug design
Proteinshop
Related services
Recent publications
Zetterberg FR, Diehl C, Håkansson M, Kahl-Knutson B, Leffler H, Nilsson UJ, Peterson K, Roper JA & Slack RJ (2023).
Discovery of Selective and Orally Available Galectin-1 Inhibitors
J. Med. Chem. https://doi.org/10.1021/acs.jmedchem.3c01787
PDB entries:
8OJP - Human galectin 1 in complex with inhibitor (on hold until publication)
A new series of orally available α-d-galactopyranosides with high affinity and specificity toward galectin-1 have been discovered. High affinity and specificity were achieved by changing six-membered aryl-triazolyl substituents in a series of recently published galectin-3-selective α-d-thiogalactosides (e.g., GB1107 Kd galectin-1/3 3.7/0.037 μM) for five-membered heterocycles such as thiazoles. One compound, GB1490 (Kd galectin-1/3 0.4/2.7 μM), was selected for further characterization toward a panel of galectins showing a selectivity of 6- to 320-fold dependent on galectin. The X-ray structure of GB1490 bound to galectin-1 reveals the compound bound in a single conformation in the carbohydrate binding site.
For other publications please see our publications page
Discovery of Selective and Orally Available Galectin-1 Inhibitors
J. Med. Chem. https://doi.org/10.1021/acs.jmedchem.3c01787
PDB entries:
8OJP - Human galectin 1 in complex with inhibitor (on hold until publication)
A new series of orally available α-d-galactopyranosides with high affinity and specificity toward galectin-1 have been discovered. High affinity and specificity were achieved by changing six-membered aryl-triazolyl substituents in a series of recently published galectin-3-selective α-d-thiogalactosides (e.g., GB1107 Kd galectin-1/3 3.7/0.037 μM) for five-membered heterocycles such as thiazoles. One compound, GB1490 (Kd galectin-1/3 0.4/2.7 μM), was selected for further characterization toward a panel of galectins showing a selectivity of 6- to 320-fold dependent on galectin. The X-ray structure of GB1490 bound to galectin-1 reveals the compound bound in a single conformation in the carbohydrate binding site.
For other publications please see our publications page
