Influence of ligand binding on structure and thermostability of human alpha(1)-acid glycoprotein
Result description
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.
Keywords
The result's identifiers
Result code in IS VaVaI
Alternative codes found
RIV/60076658:12310/16:43890978
Result on the web
DOI - Digital Object Identifier
Alternative languages
Result language
angličtina
Original language name
Influence of ligand binding on structure and thermostability of human alpha(1)-acid glycoprotein
Original language description
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.
Czech name
—
Czech description
—
Classification
Type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Recognition
ISSN
0952-3499
e-ISSN
—
Volume of the periodical
29
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
70-79
UT code for WoS article
000368640400002
EID of the result in the Scopus database
2-s2.0-84955666818
Basic information
Result type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP
CE - Biochemistry
Year of implementation
2016