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
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
收藏
页码:268 / 270
页数:3
相关论文
共 50 条
  • [41] HIV-1 protease inhibitors - A review for clinicians
    Deeks, SG
    Smith, M
    Holodniy, M
    Kahn, JO
    JAMA-JOURNAL OF THE AMERICAN MEDICAL ASSOCIATION, 1997, 277 (02): : 145 - 153
  • [42] Steroids as possible inhibitors of HIV-1 protease
    Schramm, HJ
    Quéré, L
    Büttner, J
    Wenger, T
    Dick, A
    Schramm, W
    AIDS, 1998, 12 (06) : 682 - 685
  • [43] Current development on HIV-1 protease inhibitors
    Aruksakunwong, Ornjira
    Promsri, Siriporn
    Wittayanarakul, Kitiyaporn
    Nimmanpipug, Piyarat
    Lee, Vannajan S.
    Wijitkosoom, Atchara
    Sompornpisut, Pornthep
    Hannongbua, Supot
    CURRENT COMPUTER-AIDED DRUG DESIGN, 2007, 3 (03) : 201 - 213
  • [44] CONFORMATIONALLY CONSTRAINED HIV-1 PROTEASE INHIBITORS
    VACCA, JP
    FITZGERALD, PMD
    HOLLOWAY, MK
    HUNGATE, RW
    STARBUCK, KE
    CHEN, LJ
    DARKE, PL
    ANDERSON, PS
    HUFF, JR
    BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 1994, 4 (03) : 499 - 504
  • [45] CURCUMIN DERIVATIVES AS HIV-1 PROTEASE INHIBITORS
    SUI, Z
    LI, J
    CRAIK, CS
    DEMONTELLANO, PRO
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 1993, 205 : 53 - MEDI
  • [46] APPLICATION OF HASL TO HIV-1 PROTEASE INHIBITORS
    DOWEYKO, AM
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 1992, 203 : 12 - MEDI
  • [47] Pharmacokinetic Parameters of HIV-1 Protease Inhibitors
    Nascimento, Andre L. C. S.
    Fernandes, Richard P.
    Quijia, Christian
    Araujo, Victor H. S.
    Pereira, Juliana
    Garcia, Jerusa S.
    Trevisan, Marcello G.
    Chorilli, Marius
    CHEMMEDCHEM, 2020, 15 (12) : 1018 - 1029
  • [48] Clinically effective HIV-1 protease inhibitors
    Vacca, JP
    Condra, JH
    DRUG DISCOVERY TODAY, 1997, 2 (07) : 261 - 272
  • [49] THE INHIBITORS OF THE HIV-1 POL-PROTEASE
    GUEDJ, R
    CONDOM, R
    AYI, AI
    TRAN, TT
    M S-MEDECINE SCIENCES, 1990, 6 (06): : 552 - 561
  • [50] Antimalarial activity of HIV-1 protease inhibitors
    Parikh, Sunil
    Gut, Jiri
    Istvan, Eva
    Sijwali, Puran
    Liu, Jun
    Havlir, Diane V.
    Goldberg, Daniel E.
    Rosenthal, Philip J.
    AMERICAN JOURNAL OF TROPICAL MEDICINE AND HYGIENE, 2005, 73 (06): : 110 - 111