Transformation of an antimicrobial peptide into a plasma membrane-permeable, mitochondria-targeted peptide via the substitution of lysine with arginine

Ikuhiko Nakase; Shinya Okumura; Sayaka Katayama; Hisaaki Hirose; Sílvia Pujals; Hirofumi Yamaguchi; Satoko Arakawa; Shigeomi Shimizu; Shiroh Futaki

doi:10.1039/c2cc35872g

Transformation of an antimicrobial peptide into a plasma membrane-permeable, mitochondria-targeted peptide via the substitution of lysine with arginine

Chem Commun (Camb). 2012 Nov 21;48(90):11097-9. doi: 10.1039/c2cc35872g. Epub 2012 Oct 5.

Authors

Ikuhiko Nakase¹, Shinya Okumura, Sayaka Katayama, Hisaaki Hirose, Sílvia Pujals, Hirofumi Yamaguchi, Satoko Arakawa, Shigeomi Shimizu, Shiroh Futaki

Affiliation

¹ Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan. [email protected]

PMID: 23038156
DOI: 10.1039/c2cc35872g

Abstract

Simple substitution of D-lysine with D-arginine in antimicrobial peptide (RLA) considerably improved its membrane permeability and increased mitochondrial accumulation. The potential use of RLA in preventing apoptotic cell death is also demonstrated through delivery of the Bcl-x(L) BH4 domain peptide.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Anti-Infective Agents / chemistry*
Anti-Infective Agents / toxicity
Antimicrobial Cationic Peptides / chemistry*
Antimicrobial Cationic Peptides / toxicity
Apoptosis / drug effects
Arginine / chemistry
Arginine / metabolism
Cell Membrane / metabolism
Cell Membrane Permeability
HeLa Cells
Humans
Lysine / chemistry
Lysine / metabolism
Mitochondria / metabolism*
bcl-X Protein / chemistry

Substances

Anti-Infective Agents
Antimicrobial Cationic Peptides
bcl-X Protein
Arginine
Lysine