Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

Interaction of a Potential Anticancer Agent Hypericin and its Model Compound Emodin with DNA and Bovine Serum Albumin

J. Staničová, V. Verebová, J. Beneš,

. 2018 ; 32 (5) : 1063-1070.

Jazyk angličtina Země Řecko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc19000417

BACKGROUND/AIM: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. MATERIALS AND METHODS: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. RESULTS: The strength of interaction expressed by binding constants was found to be 4.0×104 l/mol for hypericin-DNA and 8.1×104 l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. CONCLUSION: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc19000417
003      
CZ-PrNML
005      
20211223100751.0
007      
ta
008      
190107s2018 gr f 000 0|eng||
009      
AR
024    7_
$a 10.21873/invivo.11347 $2 doi
035    __
$a (PubMed)30150427
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a gr
100    1_
$a Staničová, Jana, $u Institute of Biophysics, University of Veterinary Medicine & Pharmacy, Košice, Slovakia jana.stanicova@uvlf.sk. Institute of Biophysics & Informatics, First Faculty of Medicine, Charles University, Prague, Czech Republic. $d 1960- $7 xx0267735
245    10
$a Interaction of a Potential Anticancer Agent Hypericin and its Model Compound Emodin with DNA and Bovine Serum Albumin / $c J. Staničová, V. Verebová, J. Beneš,
520    9_
$a BACKGROUND/AIM: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. MATERIALS AND METHODS: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. RESULTS: The strength of interaction expressed by binding constants was found to be 4.0×104 l/mol for hypericin-DNA and 8.1×104 l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. CONCLUSION: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate.
650    _2
$a zvířata $7 D000818
650    _2
$a protinádorové látky $x chemie $x farmakologie $7 D000970
650    _2
$a DNA $x chemie $x metabolismus $7 D004247
650    _2
$a emodin $x chemie $x farmakologie $7 D004642
650    _2
$a molekulární struktura $7 D015394
650    _2
$a perylen $x analogy a deriváty $x chemie $x farmakologie $7 D010569
650    _2
$a vazba proteinů $7 D011485
650    _2
$a sérový albumin hovězí $x chemie $x metabolismus $7 D012710
650    _2
$a spektrální analýza $7 D013057
650    _2
$a vztahy mezi strukturou a aktivitou $7 D013329
650    _2
$a termodynamika $7 D013816
655    _2
$a časopisecké články $7 D016428
700    1_
$a Verebová, Valéria $u Institute of Biophysics, University of Veterinary Medicine & Pharmacy, Košice, Slovakia. $7 xx0267732
700    1_
$a Beneš, Jiří $u Institute of Biophysics & Informatics, First Faculty of Medicine, Charles University, Prague, Czech Republic.
773    0_
$w MED00175831 $t In vivo (Athens, Greece) $x 1791-7549 $g Roč. 32, č. 5 (2018), s. 1063-1070
856    41
$u https://pubmed.ncbi.nlm.nih.gov/30150427 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20190107 $b ABA008
991    __
$a 20211223100748 $b ABA008
999    __
$a ok $b bmc $g 1364503 $s 1038540
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2018 $b 32 $c 5 $d 1063-1070 $i 1791-7549 $m In Vivo $n In Vivo $x MED00175831
LZP    __
$a Pubmed-20190107

Najít záznam

Citační ukazatele

Možnosti archivace