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Racun Tawon Brasil  membunuh sel-sel kanker

Date:

September 1, 2015

Source:

Cell Press

Summary:

tawon sosial  Polybia paulista melindungi diri terhadap predator dengan memproduksi racun yang diketahui mengandung bahan melawan kanker yang kuat . Sebuah studi baru mengungkapkan persis bagaimana racun racun ini - yang disebut MP1 ( Polybia - MP1 ) - selektif membunuh sel kanker tanpa merusak sel normal. MP1 berinteraksi dengan lipid yang abnormal didistribusikan pada permukaan sel-sel kanker , menciptakan lubang menganga yang memungkinkan molekul penting sebagai  fungsi sel untuk bocor keluar .

......... " Terapi kanker yang menyerang komposisi lipid dari membran sel akan menjadi kelas baru obat antikanker , " kata penulis studi co - senior  Paul Beales , dari University of Leeds di Inggris . " Ini bisa berguna dalam mengembangkan terapi kombinasi baru , di mana beberapa obat yang digunakan secara bersamaan untuk mengobati kanker dengan menyerang bagian yang berbeda dari sel-sel kanker pada saat yang sama . "....more

Brazilian wasp venom kills cancer cells by opening
them up

Date:

September 1, 2015

Source:

Cell Press

Summary:

The social wasp Polybia paulista
protects itself against predators by producing venom known to contain a
powerful cancer-fighting ingredient. A new study reveals exactly how the
venom's toxin -- called MP1 (Polybia-MP1) -- selectively kills cancer cells
without harming normal cells. MP1 interacts with lipids that are abnormally
distributed on the surface of cancer cells, creating gaping holes that allow
molecules crucial for cell function to leak out.

......................

The social wasp Polybia paulista protects itself against predators by producing venom
known to contain a powerful cancer-fighting ingredient. A Biophysical Journalstudy published September 1 reveals exactly how the
venom's toxin--called MP1 (Polybia-MP1)--selectively kills cancer cells without harming
normal cells. MP1 interacts with lipids that are abnormally distributed on the
surface of cancer cells, creating gaping holes that allow molecules crucial for
cell function to leak out.

"Cancer therapies that attack the
lipid composition of the cell membrane would be an entirely new class of
anticancer drugs," says co-senior study author Paul Beales, of the
University of Leeds in the UK. "This could be useful in developing new
combination therapies, where multiple drugs are used simultaneously to treat a
cancer by attacking different parts of the cancer cells at the same time."

MP1 acts against microbial pathogens by
disrupting the bacterial cell membrane. Serendipitously, the antimicrobial
peptide shows promise for protecting humans from cancer; it can inhibit the
growth of prostate and bladder cancer cells, as well as multi-drug resistant
leukemic cells. However, until now, it was not clear how MP1 selectively
destroys cancer cells without harming normal cells.

Beales and co-senior study author João
Ruggiero Neto of São Paulo State University in Brazil suspected that the reason
might have something to do with the unique properties of cancer cell membranes.
In healthy cell membranes, phospholipids called phosphatidylserine (PS) and
phosphatidylethanolamine (PE) are located in the inner membrane leaflet facing
the inside of the cell. But in cancer cells, PS and PE are embedded in the
outer membrane leaflet facing the cell surroundings.

The researchers tested their theory by
creating model membranes, some of which contained PE and/or PS, and exposing
them to MP1. They used a wide range of imaging and biophysical techniques to
characterize MP1's destructive effects on the membranes. Strikingly, the
presence of PS increased the binding of MP1 to the membrane by a factor of 7 to
8. On the other hand, the presence of PE enhanced MP1's ability to quickly
disrupt the membrane, increasing the size of holes by a factor of 20 to 30.

"Formed in only seconds, these
large pores are big enough to allow critical molecules such as RNA and proteins
to easily escape cells," Neto says. "The dramatic enhancement of the
permeabilization induced by the peptide in the presence of PE and the
dimensions of the pores in these membranes was surprising."

In future studies, the researchers plan
to alter MP1's amino acid sequence to examine how the peptide's structure
relates to its function and further improve the peptide's selectivity and
potency for clinical purposes. "Understanding the mechanism of action of
this peptide will help in translational studies to further assess the potential
for this peptide to be used in medicine," Beales says. "As it has
been shown to be selective to cancer cells and non-toxic to normal cells in the
lab, this peptide has the potential to be safe, but further work would be
required to prove that."







Story Source:

The above post is reprinted from materials provided by Cell Press. Note: Materials may be edited for content
and length.







Journal Reference:

1.   
Natália Bueno Leite, Anders
Aufderhorst-Roberts, Mario Sergio Palma, Simon D. Connell,
João Ruggiero Neto, Paul A. Beales. PE and PS Lipids
Synergistically Enhance Membrane Poration by a Peptide with Anticancer
Properties. Biophysical Journal, 2015; 109 (5): 936 DOI: 10.1016/j.bpj.2015.07.033

http://www.sciencedaily.com/releases/2015/09/150901134941.htm

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