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A contiguous stretch of methionine residues mediates the energy-dependent internalization mechanism of a cell-penetrating peptide.

Abstract：

:Recently we characterized an unusual switch in the internalization mechanism of the monomeric and dimeric forms of the cell-penetrating peptide RDLWEMMMVSLACQY. Here, we observed both energy-dependent and energy-independent modes of peptide uptake by the target B-lymphocytes WI-L2-729HF2, suggesting that higher-order structure might modulate the action of this novel cell-penetrating peptide. In the present work, we propose a possible internalization mechanism for the dimeric peptide which involves an initial interaction with the cell membrane, followed by an energy-dependent internalization process which requires the contiguous Met(6-8) sequence.

journal_name

Mol Pharm

journal_title

Molecular pharmaceutics

authors

Kim Y,Lillo A,Moss JA,Janda KD

doi

10.1021/mp050035b

keywords:

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

528-35

issue

6

eissn

1543-8384

issn

1543-8392

journal_volume

2

pub_type

杂志文章

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