Product
name: X-pep
Sequence:
MAARLCCQ
Purity: 95% by
HPLC
Counter
ion: Trifluoacetate
Format: Lyophilized
powder
Description: Cell-penetrating peptides
(CPPs) are able to penetrate the plasma membrane and gain access to the interior
of any replicating or non-replicating cell, and are being considered as drug
delivery agents. Here we describe the serendipitous discovery of a novel CPP
motif (MAARLCCQ), designated X-pep, located at the extreme N-terminus of the
X-protein of the hepatitis B virus. X-pep, and a C-terminally truncated form of
the peptide (MAARL), readily penetrated HepG2 cells. Further truncation by
removal of the terminal leucine residue impaired the cell-penetrating activity
of peptide, indicating that MAARL is the active core of the peptide. X-pep is
located adjacent to another CPP, namely Xentry, and like Xentry is unable to
penetrate unactivated resting lymphocytes suggesting selective cell uptake. A
d-isomeric form of the MAARL peptide was not cell-permeable, indicating that the
cell-penetrating function of the peptide involves stereoselective interaction
with a chiral receptor. The discovery of X-pep, which bears no resemblance to
known CPPs, allows studies to be undertaken to determine additional
characteristics of this novel CPP.
Usage: For
Scientific Research Use Only, Not for Human Use.
Reference:
Biochemical and
Biophysical Research Communications, Volume 453, Issue 1, 10 October 2014, Pages
64-68.