Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2005 Aug 2;33(13):4345–4356. doi: 10.1093/nar/gki743

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author 2005. Published by Oxford University Press. All rights reserved

The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oupjournals.org

PMC Copyright notice

Scheme 1 — Mechanism of conjugation chemistry for PNA–MTD peptides. The peptide moiety has cysteine at its N-terminus and it is activated by incorporating an -NPYS group. The PNA has a terminal cysteine at its 5′ end. In a redox reaction, the S-S linkage is formed which is stable in cell culture media but is easily degraded in the reductive intracellular environment. This degradation is critical for the peptide moiety to complete its task as a transporting vector, releasing the PNA inside the cell. Upon reduction of the disulfide bond, the PNA is released and migrates towards its target.