Prenylisoflavonoids from Erythrina senegalensis as Novel HIV-1 Protease Inhibitors

被引：32

作者：

Lee, JiSuk ^{[1
,2
]}

Oh, Won Keun ^{[3
]}

Ahn, Jong Seog ^{[3
]}

Kim, Yong Hae ^{[4
]}

Mbafor, J. Tanyi ^{[5
]}

Wandji, Jean ^{[5
]}

Fomum, Z. Tanee ^{[5
]}

机构：

[1] Seoul Natl Univ, Coll Pharm, Seoul 151742, South Korea

[2] Seoul Natl Univ, Pharmaceut Sci Res Inst, Seoul 151742, South Korea

[3] KRIBB, Taejon, South Korea

[4] Korea Adv Inst Sci & Technol, Dept Chem, Taejon 305701, South Korea

[5] Univ Yaounde, Dept Organ Chem, Yaounde, Cameroon

来源：

PLANTA MEDICA | 2009年 / 75卷 / 03期

关键词：

Erythrina senegalensis; Leguminosae; prenylated isoflavonoids; HIV-1; protease; PRENYLATED FLAVONOIDS; STEM BARK; MOGHANIA-PHILIPPINENSIS; CONSTITUENTS; 8-PRENYLLUTEONE; ISOFLAVONOIDS; ROOTS; SEEDS;

D O I：

10.1055/s-0028-1088395

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Eight compounds were isolated from the CH2Cl2 extracts of Erythrina senegalensis to assess HIV-1 protease (PR) activity inhibition. The prenylated isoflavone structures, identified by spectroscopic analysis, were 8-prenylluteone (1), auriculatin (2), erysenegalensein O (3), erysenegalensein D (4), erysenegalensein N (5), derrone (6), alpinumisoflavone (7), and 6,8-diprenylgenistein (8). The constituents showed dose-dependent inhibitory activities on HIV-1 PR with IC50 values from 0.5 to 30.0 mu M. Compounds 1-5 possessing two hydroxy groups in the 2' and 4' positions of the B ring, potently inhibited HIV-1 PR activity. In addition, 6,8-diprenylgenistein (8) with two prenyl groups in the 6 and 8 positions of the A ring and one hydroxy group in the 4' position of B-ring was the most potent HIV-1 PR inhibitor.

引用

页码：268 / 270

页数：3

共 50 条

[31] Towards the synthesis of novel boronates as potential HIV-1 protease inhibitors
Nye, Jesse L.
Clayton, Donald R.
McCammant, Matt S.
Fabry-Asztalos, Levente
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2010, 240
[32] A CONVERGENT SYNTHESIS NOVEL CONFORMATIONALLY RESTRICTED HIV-1 PROTEASE INHIBITORS
KIM, BM
GUARE, JP
HANIFIN, CM
ARFORDBICKERSTAFF, DJ
VACCA, JP
BALL, RG
TETRAHEDRON LETTERS, 1994, 35 (29) : 5153 - 5156
[33] Ionic derivatives of betulinic acid as novel HIV-1 protease inhibitors
Zhao, Hua
Holmes, Shaletha S.
Baker, Gary A.
Challa, Suresh
Bose, Himangshu S.
Song, Zhiyan
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2012, 27 (05) : 715 - 721
[34] Towards the synthesis of novel boronates as potential HIV-1 protease inhibitors
Schreiber, John D.
Faulkner, Andrea L.
Holmberg, Leah L.
Jennings, Julia J.
Frank, Michael D.
Nye, Jesse L.
Clayton, Donald R.
Fabry-Asztalos, Levente
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2011, 242
[35] Fat accumulation and HIV-1 protease inhibitors
Stricker, RB
Goldberg, B
LANCET, 1998, 352 (9137): : 1392 - 1392
[36] The Triple Threat of HIV-1 Protease Inhibitors
Potempa, Marc
Lee, Sook-Kyung
Wolfenden, Richard
Swanstrom, Ronald
FUTURE OF HIV-1 THERAPEUTICS: RESISTANCE IS FUTILE?, 2015, 389 : 203 - 241
[37] HIV-1 protease inhibitors and drug interactions
Welch, S
ADDICTION, 1997, 92 (07) : 905 - 905
[38] NONPEPTIDE COMPETITIVE INHIBITORS OF HIV-1 PROTEASE
TUMMINO, PJ
FERGUSON, D
HUPE, L
TAIT, B
HUPE, D
FASEB JOURNAL, 1994, 8 (07): : A1373 - A1373
[39] Conformational analysis of HIV-1 protease inhibitors
Brown, Jeanice
Parish, Carol A.
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2007, 233 : 52 - 52
[40] Lipopeptides as dimerization inhibitors of HIV-1 protease
Schramm, HJ
de Rosny, E
Reboud-Ravaux, M
Büttner, J
Dick, A
Schramm, W
BIOLOGICAL CHEMISTRY, 1999, 380 (05) : 593 - 596

← 1 2 3 4 5 →