Journal article
The role of alpha-helical structure in p53 peptides as a determinant for their mechanism of cell death: necrosis versus apoptosis
Advanced drug delivery reviews, v 57(4), pp 653-660
2005
PMID: 15722169
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Peptides derived from the N-terminal and C-terminal regions of the p53 tumor suppressor protein, linked to the membrane transduction domain of Antennapedia, have both been found to have significant cytotoxic effects selectively in human cancer cells. However, the N-terminal and C-terminal p53 peptides apparently display very different mechanisms for their anticancer effects. These differential effects can be attributed to dissimilar abilities to form distinctive 3-dimensional structures in extracellular-matrix-like aqueous solution that enable unique and selective cancer cell membrane penetration and effect. N-terminally based p53 peptides, with their ability to form distinctive S-shaped helix–loop–helix structures, are able to rapidly disrupt cancer cell membranes via toroidal-like pore formation causing necrosis; conversely, C-terminally based p53 peptides, due to their more random coil configuration, can be transduced across cancer cell membranes and bind to its intracellular target to cause a Fas pathway mechanism of apoptosis.
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Details
- Title
- The role of alpha-helical structure in p53 peptides as a determinant for their mechanism of cell death: necrosis versus apoptosis
- Creators
- Ramon Rosal - Columbia UniversityPaul Brandt-Rauf - Columbia UniversityMatthew R. Pincus - VA NY Harbor Healthcare SystemHsin Wang - College of Staten IslandYuehua Mao - Columbia UniversityYin Li - Columbia UniversityRobert L. Fine - Columbia University
- Publication Details
- Advanced drug delivery reviews, v 57(4), pp 653-660
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems; Drexel University
- Web of Science ID
- WOS:000227570500012
- Scopus ID
- 2-s2.0-13844255513
- Other Identifier
- 991019323675904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Pharmacology & Pharmacy