Bio-ihletésű fémkötő peptidek alkalmazása a metalloenzimek funkcionális modellezésénél = Bioinspired metallopeptides for the functional mimicking of metalloenzymes

Munkank soran szamos metalloprotein/enzim femkotő szekvenciajaval azonos oligopeptidet allitottunk elő es vizsgaltuk azok femkotő es enzimutanzo sajatsagait. Az eredmenyek hozzajarultak a vizsgalt feherjek (human endostatin, human hisztidin-gazdag glikoprotein (HRG), ket Gram-negativ patogen bakterium Cu,Zn-SOD-ja) tulajdonsagainak, műkodesenek, femion-felveteli folyamatainak jobb megertesehez. Az altalunk korabban es a jelen projektben vizsgalt femkotő oligopeptidek sajatsagainak ismereteben tobb peptidalapu, biomimetikus enzim modellt is terveztunk, melyek utanozni kepesek a metalloproteinek aktiv centrumaban kialakulo femion kornyezetet. E modellek kozul tobb is hatekonynak mutatkozott mind hidrolitikus, mind oxidativ folyamatok katalizisere. Fentiek mellett tobb, nem-peptid tipusu tobbmagvu femkomplexek kialakitasara alkalmas ligandumot vizsgaltunk, melyek hatekonyan es (bazis)szelektiven kepesek foszforsavmonoeszterek es az RNS hidroliziset elősegiteni. | During our work we prepared a number of oligopeptides with sequences identical to the meta binding sites of some selected metalloproteines/enzymes, and we studied their interactions with metal ions, as well as the enzyme mimicking ability of their metal complexes. Our results contributed to the understanding the properties, the catalytic mechanisms and metal uptake processes of the mimicked proteins (human endostatin, human histidine-rich glycoprotein (HRG), two Gram-negative patogen bacterial Cu,Zn-SOD). Based on the metal binding properties of the peptides studied by us (earlier or in this project) we designed some peptide based, biomimetic enzyme models, which are able to mimic the metal ion environment in the active sites of metalloenzymes. Some of these models have notable activity in promoting both hydrolytic and oxidative reactions. Besides, we designed several non-peptide based, dinucleating ligands, too. The Cu(II) and Zn(II) complexes of these ligands are able to promote (base)selective hydrolysis of both phosphomonoesters and RNAs.