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Backbone rigidity and static presentation of guanidinium groups increases cellular uptake of arginine-rich cell-penetrating peptides
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2011 (English)In: Nature Communications, ISSN 2041-1723, Vol. 2, 453- p.Article in journal (Refereed) Published
Abstract [en]

In addition to endocytosis-mediated cellular uptake, hydrophilic cell-penetrating peptides are able to traverse biological membranes in a non-endocytic mode termed transduction, resulting in immediate bioavailability. Here we analysed structural requirements for the non-endocytic uptake mode of arginine-rich cell-penetrating peptides, by a combination of live-cell microscopy, molecular dynamics simulations and analytical ultracentrifugation. We demonstrate that the transduction efficiency of arginine-rich peptides increases with higher peptide structural rigidity. Consequently, cyclic arginine-rich cell-penetrating peptides showed enhanced cellular uptake kinetics relative to their linear and more flexible counterpart. We propose that guanidinium groups are forced into maximally distant positions by cyclization. This orientation increases membrane contacts leading to enhanced cell penetration.

Place, publisher, year, edition, pages
2011. Vol. 2, 453- p.
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Natural Sciences
URN: urn:nbn:se:su:diva-68314DOI: 10.1038/ncomms1459ISI: 000294806500046OAI: diva2:477415
authorCount :8Available from: 2012-01-13 Created: 2012-01-03 Last updated: 2012-01-13Bibliographically approved

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