TY  - JOUR
AU  - Hetényi, Anasztázia
AU  - Hegedüs, Zsófia
AU  - Fajka-Boja, Roberta
AU  - Monostori, Éva
AU  - E Kövér, Katalin
AU  - Martinek, Tamás
TI  - Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD
JF  - JOURNAL OF BIOMOLECULAR NMR
J2  - J BIOMOL NMR
VL  - 66
PY  - 2016
IS  - 4
SP  - 227
EP  - 232
PG  - 6
SN  - 0925-2738
DO  - 10.1007/s10858-016-0076-3
UR  - https://m2.mtmt.hu/api/publication/3148106
ID  - 3148106
N1  - Funding Agency and Grant Number: Hungarian Research Foundation OTKA [PD83600, K105459]; Hungarian Academy of Sciences, Lendulet program [LP-2011-009]; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/2-11/1-2012-0001]; EU; European Regional Development Fund [GINOP-2.3.3-15-2016-00004, GINOP-2.3.3-15-2016-00010]\n Funding text: This work was supported by the Hungarian Research Foundation OTKA projects PD83600 and K105459 and the Hungarian Academy of Sciences, Lendulet program (LP-2011-009). This research was supported by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TAMOP-4.2.4.A/2-11/1-2012-0001 'National Excellence Program'. The research was supported by the EU and co-financed by the European Regional Development Fund under the projects GINOP-2.3.3-15-2016-00004 and GINOP-2.3.3-15-2016-00010.\n
Funding Agency and Grant Number: Hungarian Research Foundation OTKA [PD83600, K105459]; Hungarian Academy of Sciences, Lendulet program [LP-2011-009]; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/2-11/1-2012-0001]; EU; European Regional Development Fund [GINOP-2.3.3-15-2016-00004, GINOP-2.3.3-15-2016-00010]
            Funding text: This work was supported by the Hungarian Research Foundation OTKA projects PD83600 and K105459 and the Hungarian Academy of Sciences, Lendulet program (LP-2011-009). This research was supported by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TAMOP-4.2.4.A/2-11/1-2012-0001 'National Excellence Program'. The research was supported by the EU and co-financed by the European Regional Development Fund under the projects GINOP-2.3.3-15-2016-00004 and GINOP-2.3.3-15-2016-00010.
AB  - Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein-ligand interactions is a key element. H-1 saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed N-15-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A N-15-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system.
LA  - English
DB  - MTMT
ER  -