Document Detail


Anticancer peptide SVS-1: efficacy precedes membrane neutralization.
MedLine Citation:
PMID:  22839778     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Anticancer peptides are polycationic amphiphiles capable of preferentially killing a wide spectrum of cancer cells relative to noncancerous cells. Their primary mode of action is an interaction with the cell membrane and subsequent activation of lytic effects; however, the exact mechanism responsible for this mode of action remains controversial. Using zeta potential analyses we demonstrate the interaction of a small anticancer peptide with membrane model systems and cancer cells. Electrostatic interactions have a pivotal role in the cell killing process, and in contrast to the antimicrobial peptides action cell death occurs without achieving full neutralization of the membrane charge.
Authors:
Diana Gaspar; Ana Salomé Veiga; Chomdao Sinthuvanich; Joel P Schneider; Miguel A R B Castanho
Related Documents :
21802268 - Antidepressant-like effect of hyperoside isolated from apocynum venetum leaves: possibl...
21603238 - Comparison of in leakage from labeled endocardial and epicardial cells: impact on model...
15084638 - Noradrenergic induction of selective plasticity in the frequency tuning of auditory cor...
21728238 - Truly nonionic polymer shells for the encapsulation of living cells.
16846658 - Statistical parametric mapping of immunopositive cell density.
3602988 - Mixed follicular-parafollicular carcinoma of the thyroid.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't     Date:  2012-08-03
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-09-20     Completed Date:  2012-10-29     Revised Date:  2013-08-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6263-5     Citation Subset:  IM    
Affiliation:
Instituto de Medicina Molecular, Faculdade de Medicina da Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antineoplastic Agents / chemistry,  pharmacology*
Cell Death / drug effects
Cell Line, Tumor
Humans
Inhibitory Concentration 50
Membranes, Artificial
Peptides / chemistry,  pharmacology*
Phosphatidylcholines / chemistry
Phosphatidylserines / chemistry
Static Electricity
Stereoisomerism
Grant Support
ID/Acronym/Agency:
ZIA BC011314-02/BC/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antineoplastic Agents; 0/Membranes, Artificial; 0/Peptides; 0/Phosphatidylcholines; 0/Phosphatidylserines; 0/SVS-1 peptide; 40290-44-6/1-palmitoyl-2-oleoylglycero-3-phosphoserine; TE895536Y5/1-palmitoyl-2-oleoylphosphatidylcholine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Patterns and architecture of genomic islands in marine bacteria.
Next Document:  VtaA8 and VtaA9 from Haemophilus parasuis delay phagocytosis by alveolar macrophages.