Influence of ligand binding on structure and thermostability of human alpha(1)-acid glycoprotein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00463165" target="_blank" >RIV/61388971:_____/16:00463165 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/16:43890978

Výsledek na webu

<a href="http://dx.doi.org/10.1002/jmr.2496" target="_blank" >http://dx.doi.org/10.1002/jmr.2496</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jmr.2496" target="_blank" >10.1002/jmr.2496</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Influence of ligand binding on structure and thermostability of human alpha(1)-acid glycoprotein

Popis výsledku v původním jazyce

Ligand binding of neutral progesterone, basic propranolol, and acidic warfarin to human alpha(1)-acid glycoprotein (AGP) was investigated by Raman spectroscopy. The binding itself is characterized by a uniform conformational shift in which a tryptophan residue is involved. Slight differences corresponding to different contacts of the individual ligands inside the beta-barrel are described. Results are compared with in silico ligand docking into the available crystal structure of deglycosylated AGP using quantum/molecular mechanics. Calculated binding energies are -18.2, -14.5, and -11.5 kcal/mol for warfarin, propranolol, and progesterone, respectively. These calculations are consistent with Raman difference spectroscopy; nevertheless, minor discrepancies in the precise positions of the ligands point to structural differences between deglycosylated and native AGP.

Název v anglickém jazyce

Influence of ligand binding on structure and thermostability of human alpha(1)-acid glycoprotein

Popis výsledku anglicky

Ligand binding of neutral progesterone, basic propranolol, and acidic warfarin to human alpha(1)-acid glycoprotein (AGP) was investigated by Raman spectroscopy. The binding itself is characterized by a uniform conformational shift in which a tryptophan residue is involved. Slight differences corresponding to different contacts of the individual ligands inside the beta-barrel are described. Results are compared with in silico ligand docking into the available crystal structure of deglycosylated AGP using quantum/molecular mechanics. Calculated binding energies are -18.2, -14.5, and -11.5 kcal/mol for warfarin, propranolol, and progesterone, respectively. These calculations are consistent with Raman difference spectroscopy; nevertheless, minor discrepancies in the precise positions of the ligands point to structural differences between deglycosylated and native AGP.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Recognition

ISSN

0952-3499

e-ISSN

—

Svazek periodika

29

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

70-79

Kód UT WoS článku

000368640400002

EID výsledku v databázi Scopus

2-s2.0-84955666818