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Issue 33, 2012
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Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air–water interface

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Abstract

We have designed heparin-incorporated model lipid monolayers and monitored the adsorption behaviours of cell penetrating peptides (CPPs) on a molecular scale at the air–water interface. We found initially that heparin could incorporate homogeneously into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dipalmitoyl-sn-glycero-3-phosphoserine (DPPS), and DPPC/DPPS mixed monolayers, allowing improved adsorption of transcription-activating factor (TAT) derived peptide (TAT-TDP) molecules. X-ray reflectivity measurements, as well as the surface pressure changes from surface pressure–area isotherms, suggest that a preferred interaction of heparin with TAT-TDP occurs, and is responsible for the effective penetration. This behaviour resembles the ubiquitous activities of glycosaminoglycan (GAG) molecules as cellular receptors that promote intracellular transport of cell-penetrating peptide domains in biological systems. We suggest that heparin–TAT-TDP complex formation can be exploited in a primary step of CPP translocation.

Graphical abstract: Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air–water interface

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Publication details

The article was received on 16 Apr 2012, accepted on 11 Jun 2012 and first published on 20 Jul 2012


Article type: Paper
DOI: 10.1039/C2SM25885D
Citation: Soft Matter, 2012,8, 8616-8623

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    Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air–water interface

    D. Hong, K. Shin, M. James and G. Tae, Soft Matter, 2012, 8, 8616
    DOI: 10.1039/C2SM25885D

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