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Lawrence N, Philippe GJ, Harvey PJ, et al. Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells. RSC Chem Biol. 2020;1(5):405-420doi: 10.1039/d0cb00099j.
Lawrence, N., Philippe, G. J., Harvey, P. J., Condon, N. D., Benfield, A. H., Cheneval, O., Craik, D. J., & Troeira Henriques, S. (2020). Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells. RSC chemical biology, 1(5), 405-420. https://doi.org/10.1039/d0cb00099j
Lawrence, Nicole, et al. "Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells." RSC chemical biology vol. 1,5 (2020): 405-420. doi: https://doi.org/10.1039/d0cb00099j
Lawrence N, Philippe GJ, Harvey PJ, Condon ND, Benfield AH, Cheneval O, Craik DJ, Troeira Henriques S. Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells. RSC Chem Biol. 2020 Oct 20;1(5):405-420. doi: 10.1039/d0cb00099j. eCollection 2020 Dec 01. PMID: 34458771; PMCID: PMC8386104.
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RSC Chem Biol. 2020 Oct 20;1(5):405-420. doi: 10.1039/d0cb00099j. eCollection 2020 Dec 01.

Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells.

RSC chemical biology

Nicole Lawrence, Grégoire J-B Philippe, Peta J Harvey, Nicholas D Condon, Aurélie H Benfield, Olivier Cheneval, David J Craik, Sónia Troeira Henriques

Affiliations

  1. Institute for Molecular Bioscience, The University of Queensland Brisbane Queensland 4072 Australia [email protected] [email protected] [email protected] +61 7 34437342 +61 7 33462014 +61 7 33462019.
  2. Queensland University of Technology, School of Biomedical Sciences, Institute of Health & Biomedical Innovation and Translational Research Institute Brisbane Queensland 4102 Australia.

PMID: 34458771 PMCID: PMC8386104 DOI: 10.1039/d0cb00099j

Abstract

Cell penetrating peptides (CPPs) are valuable tools for developing anticancer therapies due to their ability to access intracellular targets, including protein-protein interactions. cPF4PD is a newly described CPP designed from a transduction domain of the human defense protein platelet factor 4 (PF4), that also has antimalarial activity. The cPF4PD peptide recapitulates the helical structure of the PF4 domain and maintains activity against intracellular malaria parasites

This journal is © The Royal Society of Chemistry.

Conflict of interest statement

There are no conflicts to declare.

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