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

Youngsoo Kim, Antonietta Lillo, Jason A. Moss, Kim D. Janda

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)528-535
Number of pages8
JournalMolecular Pharmaceutics
Volume2
Issue number6
DOIs
Publication statusPublished - 2005 Nov

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery

Fingerprint Dive into the research topics of 'A contiguous stretch of methionine residues mediates the energy-dependent internalization mechanism of a cell-penetrating peptide'. Together they form a unique fingerprint.

  • Cite this