How does BIRD-2 peptide kill B-cell lymphoma?

The anti-apoptotic factor Bcl-2 is over-expressed in B-cell lymphoma cells as their main survival mechanism by binding to IP3R2 on endoplasmic reticulum (ER).  In this study, a cell-penetrating version of BIRD-2 peptide (Bcl-2/IP3R Disrupter-2 peptide with a TAT sequence) made by LifeTein was used to break up the complex formed by Bcl-2 and IP3R2 in human diffuse large B-cell lymphoma (DLBCL) cells. Ca2+ signaling-related events are suggested to be the killing mechanism of BIRD-2 peptide on DLBCL cells.

Bird-2 Peptides & B-Cell Lymphoma

[PDF] Inhibiting Bcl-2 via its BH4 domain in DLBCL cancers to provoke pro-apoptotic Ca2+ signaling

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LifeTein Launches Rush Custom Peptide Synthesis Service: Peptide Delivered in 3-5 Days

Peptide Synthesis for Cell-penetration Studies

Cell-penetrating peptides (CPPs) have the ability to enter a cell’s plasma membrane independent of a membrane receptor. Attached to a CPP, therapeutic cargo could be delivered to an intracellular target, thus overcoming the entry restrictions set by the plasma membrane.

Peptide Synthesis & Cell Penetration

The cationic CPPs interact with negatively charged head groups of lipids directly in the plasma membrane through electrostatic interactions. The increased local peptide concentration at the membrane surface will cause a transient destabilization of the lipid bilayer and lead to cell entry. The hydrophobic interactions, especially facilitated by the presence of tryptophan residues, may be important for the CPP-membrane interaction and cellular internalization.

Please click here for more details for cell penetrating peptide synthesis services: http://lifetein.com/Cell_Penetrating_Peptides.html

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