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It is becoming increasingly clear that plants ranging 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.

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Faculty of Technology ePrints Service  


Harris, Frederick -  Prabhu, Saurabh -  R. Dennison, Sarah -  J. Snape, Timothy -  Lea, Robert -  Mura, Manuela -  A. Phoenix, David - 

Id.: 69957518

Idioma: inglés  -  inglés  - 

Versión: 1.0

Estado: Final

Tipo:  application/pdf -  application/msword - 

Palabras claveB200 Pharmacology, Toxicology and Pharmacy - 

Tipo de recurso: Article  -  PeerReviewed  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

Formatos:  application/pdf -  application/msword - 

Requerimientos técnicos:  Browser: Any - 

Relación: [References] http://eprints.lincoln.ac.uk/27986/
[References] 10.2174/0929866523666160511151215

Fecha de contribución: 26-sep-2017


* Harris, Frederick and Prabhu, Saurabh and R. Dennison, Sarah and J. Snape, Timothy and Lea, Robert and Mura, Manuela and A. Phoenix, David (2016) Anionic host defence peptides from the plant kingdom: their anticancer activity and mechanisms of action. Protein & Peptide Letters, 23 (8). pp. 676-687. ISSN 0929-8665

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