Next Article in Journal
Synthesis and Neuroprotective Action of Optically Pure Neoechinulin A and Its Analogs
Next Article in Special Issue
Imperatoxin A, a Cell-Penetrating Peptide from Scorpion Venom, as a Probe of Ca2+-Release Channels/Ryanodine Receptors
Previous Article in Journal
Beta-Adrenergic Agonists
Previous Article in Special Issue
Cell-Penetrating Peptides—Mechanisms of Cellular Uptake and Generation of Delivery Systems
Article Menu

Export Article

Open AccessArticle
Pharmaceuticals 2010, 3(4), 1045-1062;

Cell-Penetrating Peptides: A Comparative Study on Lipid Affinity and Cargo Delivery Properties

Institute of Biomolecular Chemistry of CNR, Padova Unit, and Department of Chemical Sciences, University of Padova, via Marzolo 1, I-35131 Padova, Italy
Author to whom correspondence should be addressed.
Received: 22 December 2009 / Revised: 23 March 2010 / Accepted: 29 March 2010 / Published: 30 March 2010
(This article belongs to the Special Issue Cell-penetrating Peptides 2012)
Full-Text   |   PDF [399 KB, uploaded 1 April 2010]   |  


A growing number of natural and/or synthetic peptides with cell membrane penetrating capability have been identified and described in the past years. These molecules have been considered promising tools for delivering bioactive compounds into various cell types. Although the mechanism of uptake is still unclear, it is reasonable to assume that the relative contribute of each proposed mechanism could differ for the same peptide, depending on experimental protocol and cargo molecule composition. In this work we try to connect the capability to interact with model lipid membrane and structural and chemical characteristics of CPPs in order to obtain a biophysical classification that predicts the behavior of CPP-cargo molecules in cell systems. Indeed, the binding with cell membrane is one of the primary step in the interaction of CPPs with cells, and consequently the studies on model membrane could become important for understanding peptide-membrane interaction on a molecular level, explaining how CPPs may translocate a membrane without destroying it and how this interactions come into play in shuttling CPPs via different routes with different efficiency. We analyzed by CD and fluorescence spectroscopies the binding properties of six different CPPs (kFGF, Nle54-Antp and Tat derived peptides, and oligoarginine peptides containing 6, 8 or 10 residues) in absence or presence of the same cargo peptide (the 392-401pTyr396 fragment of HS1 protein). The phospholipid binding properties were correlated to the conformational and chemical characteristics of peptides, as well as to the cell penetrating properties of the CPP-cargo conjugates. Results show that even if certain physico-chemical properties (conformation, positive charge) govern CPP capability to interact with the model membrane, these cannot fully explain cell-permeability properties. View Full-Text
Keywords: antennapedia; kFGF; Tat; poly-arginine peptides; conformational studies; lipid affinity antennapedia; kFGF; Tat; poly-arginine peptides; conformational studies; lipid affinity

Figure 1

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Ruzza, P.; Biondi, B.; Marchiani, A.; Antolini, N.; Calderan, A. Cell-Penetrating Peptides: A Comparative Study on Lipid Affinity and Cargo Delivery Properties. Pharmaceuticals 2010, 3, 1045-1062.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Pharmaceuticals EISSN 1424-8247 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top