Studies on anticancer activities of antimicrobial peptides

被引:1020
作者
Hoskin, David W. [1 ]
Ramamoorthy, Ayyalusamy [2 ]
机构
[1] Dalhousie Univ, Fac Med, Dept Pathol, Dept Microbiol & Immunol, Halifax, NS B3H 1X5, Canada
[2] Univ Michigan, Dept Chem & Biophys, Ann Arbor, MI 48109 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2008年 / 1778卷 / 02期
关键词
antimicrobial peptide; anticancer peptide; membrane; lipid bilayer; drug;
D O I
10.1016/j.bbamem.2007.11.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In spite of great advances in cancer therapy, there is considerable current interest in developing anticancer agents with a new mode of action because of the development of resistance by cancer cells towards current anticancer drugs. A growing number of studies have shown that some of the cationic antimicrobial peptides (AMPs), which are toxic to bacteria but not to normal mammalian cells, exhibit a broad spectrum of cytotoxic activity against cancer cells. Such studies have considerably enhanced the significance of AMPs, both synthetic and from natural sources, which have been of importance both for an increased understanding of the immune system and for their potential as clinical antibiotics. The electrostatic attraction between the negatively charged components of bacterial and cancer cells and the positively charged AMPs is believed to play a major role in the strong binding and selective disruption of bacterial and cancer cell membranes, respectively. However, it is unclear why some host defense peptides are able to kill cancer cells when others do not. In addition, it is not clear whether the molecular mechanism(s) underlying the antibacterial and anticancer activities of AMPs are the same or different. In this article, we review various studies on different AMPs that exhibit cytotoxic activity against cancer cells. The suitability of cancer cell-targeting AMPs as cancer therapeutics is also discussed. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:357 / 375
页数:19
相关论文
共 207 条
  • [1] Adamia Sophia, 2005, Current Drug Targets - Cardiovascular & Haematological Disorders, V5, P3, DOI 10.2174/1568006053005056
  • [2] AMINO-ACID-SEQUENCE OF PR-39 - ISOLATION FROM PIG INTESTINE OF A NEW MEMBER OF THE FAMILY OF PROLINE-ARGININE-RICH ANTIBACTERIAL PEPTIDES
    AGERBERTH, B
    LEE, JY
    BERGMAN, T
    CARLQUIST, M
    BOMAN, HG
    MUTT, V
    JORNVALL, H
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 202 (03): : 849 - 854
  • [3] Allred LE, 1979, SURFACES NORMAL MALI, P21
  • [4] Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface
    Andersen, JH
    Jenssen, H
    Sandvik, K
    Gutteberg, TJ
    [J]. JOURNAL OF MEDICAL VIROLOGY, 2004, 74 (02) : 262 - 271
  • [5] Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts
    Andersen, JH
    Osbakk, SA
    Vorland, LH
    Traavik, T
    Gutteberg, TJ
    [J]. ANTIVIRAL RESEARCH, 2001, 51 (02) : 141 - 149
  • [6] SHORTENED CECROPIN-A MELITTIN HYBRIDS - SIGNIFICANT SIZE-REDUCTION RETAINS POTENT ANTIBIOTIC-ACTIVITY
    ANDREU, D
    UBACH, J
    BOMAN, A
    WAHLIN, B
    WADE, D
    MERRIFIELD, RB
    BOMAN, HG
    [J]. FEBS LETTERS, 1992, 296 (02) : 190 - 194
  • [7] BAKER MA, 1993, CANCER RES, V53, P3052
  • [8] Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
    Bechinger, B
    Zasloff, M
    Opella, SJ
    [J]. BIOPHYSICAL JOURNAL, 1998, 74 (02) : 981 - 987
  • [9] STRUCTURE AND ORIENTATION OF THE ANTIBIOTIC PEPTIDE MAGAININ IN MEMBRANES BY SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
    BECHINGER, B
    ZASLOFF, M
    OPELLA, SJ
    [J]. PROTEIN SCIENCE, 1993, 2 (12) : 2077 - 2084
  • [10] Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    Bechinger, Burkhard
    Lohner, Karl
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2006, 1758 (09): : 1529 - 1539