LOGIN TO YOUR ACCOUNT

Username
Password
Remember Me
Or use your Academic/Social account:

CREATE AN ACCOUNT

Or use your Academic/Social account:

Congratulations!

You have just completed your registration at OpenAire.

Before you can login to the site, you will need to activate your account. An e-mail will be sent to you with the proper instructions.

Important!

Please note that this site is currently undergoing Beta testing.
Any new content you create is not guaranteed to be present to the final version of the site upon release.

Thank you for your patience,
OpenAire Dev Team.

Close This Message

CREATE AN ACCOUNT

Name:
Username:
Password:
Verify Password:
E-mail:
Verify E-mail:
*All Fields Are Required.
Please Verify You Are Human:
fbtwitterlinkedinvimeoflicker grey 14rssslideshare1
Harris, Frederick; Prabhu, Saurabh; R. Dennison, Sarah; J. Snape, Timothy; Lea, Robert; Mura, Manuela; A. Phoenix, David (2016)
Publisher: Bentham Science Publishers
Languages: English
Types: Article
Subjects: C770, B200 Pharmacology, Toxicology and Pharmacy, C720

Classified by OpenAIRE into

mesheuropmc: food and beverages
It is becoming increasingly clear that plants, ranging from across the plant kingdom produce anionic host defence peptides (AHDPs) with potent activity against a wide variety of human cancers cells. In general, this activity involves membrane partitioning by AHDPs, which leads to membranolysis and / or internalization to attack intracellular targets such as DNA. Several models have been proposed to describe these events including: the toroidal pore and Shai-Matsuzaki-Huang mechanisms but, in general, the mechanisms underpinning the membrane interactions and anticancer activity of these peptides are poorly understood. Plant AHDPs with anticancer activity can be conveniently discussed with reference to two groups: cyclotides, which possess cyclic molecules stabilized by cysteine knot motifs, and other ADHPs that adopt extended and α-helical conformations. Here, we review research into the anticancer action of these two groups of peptides along with current understanding of the mechanisms underpinning this action.
  • The results below are discovered through our pilot algorithms. Let us know how we are doing!

    • Phoenix, D.A., S.R. Dennison, and F. Harris, Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity, in Antimicrobial Peptides. 2013, Wiley-VCH Verlag GmbH & Co. KGaA. p. 1-37.
    • Jones, J.D.G. and J.L. Dangl, The plant immune system. Nature, 2006. 444(7117): p.
    • Spoel, S.H. and X. Dong, How do plants achieve immunity? Defence without specialized immune cells. Nature Reviews Immunology, 2012. 12(2): p. 89-100.
    • Sels, J., et al., Plant pathogenesis-related (PR) proteins: A focus on PR peptides. Plant Physiology and Biochemistry, 2008. 46(11): p. 941-950.
    • De Lucca, A.J., T.E. Cleveland, and D.E. Wedge, Plant-derived antifungal proteins and peptides. Can J Microbiol, 2005. 51(12): p. 1001-1014.
    • Borad, V. and S. Sriram, Pathogenesis-Related Proteins for the Plant Protection. Asian Journal of Experimental Sciences, 2008. 22(3): p. 189-196.
    • Edreva, A., Pathogenesis-related proteins: Research progress in the last 15 years.
    • General Applied Plant Physiology. , 2005. 31(1-2): p. 105-124.
    • van Loon, L.C., M. Rep, and C.M.J. Pieterse, Significance of inducible defense-related proteins in infected plants, in Annual Review of Phytopathology. 2006. p. 135-162.
    • Van Loon, L.C. and E.A. Van Strien, The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiological and Molecular Plant Pathology, 1999. 55(2): p. 85-97.
    • Ribeiro, S.M., S.C. Dias, and O.L. Franco, Plant Antimicrobial Peptides: From Basic Structures to Applied Research, in Peptide Drug Discovery and Development. 2011, Wiley-VCH Verlag GmbH & Co. KGaA. p. 139-155.
    • Peptides, 2008. 29(10): p. 1842-1851.
    • Barbosa Pelegrini, P., et al., Antibacterial peptides from plants: what they are and how they probably work. Biochemistry research international, 2011. 2011: p. 250349.
    • Nucleic Acids Res, 2009. 37(Database issue): p. D963-8.
    • Carvalho, A.d.O. and V.M. Gomes, Plant defensins and defensin-like peptides - biological activities and biotechnological applications. Current pharmaceutical design, 2011. 17(38): p. 4270-93.
    • Merillon and K.G. Ramawat, Editors. 2012. p. 333-344.
    • Egorov, T.A. and T.I. Odintsova, Defense Peptides of Plant Immunity. Russian Journal of Bioorganic Chemistry, 2012. 38(1): p. 1-9.
    • FEBS Letters, 2011. 585(7): p. 995-1000.
    • Benko-Iseppon, A.M., et al., Overview on Plant Antimicrobial Peptides. Current Protein & Peptide Science, 2010. 11(3): p. 181-188.
    • Padovan, L., M. Scocchi, and A. Tossi, Structural Aspects of Plant Antimicrobial Peptides. Current Protein & Peptide Science, 2010. 11(3): p. 210-219.
    • López-García, B., B.S. Segundo, and M. Coca, Antimicrobial Peptides as a Promising Alternative for Plant Disease Protection, in Small Wonders: Peptides for Disease Control. 2012, American Chemical Society. p. 263-294.
    • Svetlana, O., H. Jong Hyun, and C. Marc Alan, Thionins - Nature?s Weapons of Mass Protection, in Small Wonders: Peptides for Disease Control. 2012, American Chemical Society. p. 415-443.
    • Prabhu, S., et al., Anionic Antimicrobial and Anticancer Peptides from Plants. Critical Reviews in Plant Sciences, 2013. 32(5): p. 303-320.
    • Harris, F., S.R. Dennison, and D.A. Phoenix, Anionic Antimicrobial Peptides from Eukaryotic Organisms. Current Protein & Peptide Science, 2009. 10(6): p. 585-606.
    • Wang, G., X. Li, and Z. Wang, APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Research, 2009. 37: p. D933-D937.
    • Wang, G., X. Li, and M. Zasloff, A Database View of Naturally Occurring Antimicrobial Peptides: Nomenclature, Classification and Amino Acid Sequence Analysis. Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies, ed. G. Wang. 2010. 1-21.
    • Sarika, M.A. Iquebal, and A. Rai, Biotic stress resistance in agriculture through antimicrobial peptides. Peptides, 2012. 36(2): p. 322-330.
    • Harris, F., S.R. Dennison, and D.A. Phoenix, Anionic Antimicrobial Peptides from Eukaryotic Organisms and their Mechanisms of Action. Current Chemical Biology, 2011. 5(2): p. 142-153.
    • Phoenix, D.A., S.R. Dennison, and F. Harris, Anionic Antimicrobial Peptides, in Antimicrobial Peptides. 2013, Wiley-VCH Verlag GmbH & Co. KGaA. p. 83-113.
    • DOI: 10.1002/9783527652853.ch3 (available at: http://onlinelibrary.wiley.com/doi/10.1002/9783527652853.ch3/summary)
  • No related research data.
  • No similar publications.