Investigation of new indole derivatives of bovine serum albumin using spectroscopic and molecular docking techniques

被引：5

作者：

Dezhampanah, H. ^{[1
]}

Esmaili, M. ^{[1
]}

Dafrazi, A. Akbarnia ^{[1
]}

Mehdizadeh, P. ^{[1
]}

机构：

[1] Univ Guilan, Dept Chem, Phys Chem Lab, Fac Sci, POB 41335-1914, Rasht 0098, Iran

来源：

BIOTECHNIC & HISTOCHEMISTRY | 2019年 / 94卷 / 03期

关键词：

Bis(indolyl)methane; bovine serum albumin; docking study; F0rster energy transfer; molecular modeling; BINDING INTERACTION; FLUORESCENCE; FLAVONOIDS; APOPTOSIS; GROWTH; PH;

D O I：

10.1080/10520295.2018.1537510

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We investigated the interaction of two derivatives of bis (indolyl) methane with bovine serum albumin (BSA) using spectroscopic and molecular docking calculations. Fluorescence quenching measurements revealed that the quenching mechanism was static. F0rster energy transfer measurements, synchronous fluorescence spectroscopy and docking studies demonstrated that both bis(indolyl)methanes bound to the Trp residues of BSA. The docking study confirmed that both bis(indolyl)methanes form hydrogen bonds and van der Waals interactions with BSA. Our molecular docking study indicated that the compounds are located within the binding pocket of subdomains IIB and IB of BSA. Fourier transform infrared spectroscopy demonstrated that both bis(indolyl)methane derivatives can interact with BSA and can affect the secondary structure of BSA.

引用

页码：167 / 179

页数：13

共 36 条

[11] 1,1-Bis(3'-indolyl)-1-(p-methoxyphenyl)methane activates Nur77-independent proapoptotic responses in colon cancer cells [J].

Cho, Sung Dae ;

Lei, Ping ;

Abdelrahim, Maen ;

Yoon, Kyungsil ;

Liu, Shengxi ;

Guo, Jingjing ;

Papineni, Sabitha ;

Chintharlapalli, Sudhakar ;

Safe, Stephen .

MOLECULAR CARCINOGENESIS, 2008, 47 (04) :252-263

[12]

Fasman DG, 1992, PRACTICAL HDB BIOCH, V26, P42

[13]

Gordon G, 2010, HETEROCYCLIC SCAFFOL, V26, P42

[14] RAPID CONFIRMATION AND REVISION OF THE PRIMARY STRUCTURE OF BOVINE SERUM-ALBUMIN BY ESIMS AND FRIT-FAB LC MS [J].

HIRAYAMA, K ;

AKASHI, S ;

FURUYA, M ;

FUKUHARA, K .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1990, 173 (02) :639-646

[15] Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: A spectroscopic study in combination with molecular docking and molecular dynamics simulation [J].

Jana, Sankar ;

Dalapati, Sasanka ;

Ghosh, Shalini ;

Guchhait, Nikhil .

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY, 2012, 231 (01) :19-27

[16] Inhibition of bladder tumor growth by 1,1-bis(3′-indolyl)-1-(p-substitutedphenyl)methanes:: A new class of peroxisome proliferator-activated receptor γ agonists [J].

Kassouf, W ;

Chintharlapalli, S ;

Abdelrahim, M ;

Nelkin, G ;

Safe, S ;

Kamat, AM .

CANCER RESEARCH, 2006, 66 (01) :412-418

[17] Zirconium(IV)-catalyzed one-pot synthesis and oxidation of bis- and tris(indolyl)methanes into conjugated chromophores as new pH indicators or calorimetric chemosensors for transition metals [J].

Khorshidi, Alireza ;

Mardazad, Neda ;

Shaabanzadeh, Zahra .

TETRAHEDRON LETTERS, 2014, 55 (29) :3873-3877

[18]

KRAGHHANSEN U, 1981, PHARMACOL REV, V33, P17

[19]

Lakowicz J.R., 2013, Principles of fluorescence spectroscopy, P445

[20] Structural Relationship and Binding Mechanisms of Five Flavonoids with Bovine Serum Albumin [J].

Liu, E-Hu ;

Qi, Lian-Wen ;

Li, Ping .

MOLECULES, 2010, 15 (12) :9092-9103

← 1 2 3 4 →