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Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/5450

Title: Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air-water interface
Authors: Hong, D
Shin, K
James, M
Tae, G
Keywords: PEPTIDES
X-RAY LASERS
LIPIDS
MEMBRANES
SURFACES
ISOTHERMS
Issue Date: 1-Jan-2012
Publisher: ROYAL SOCIETY OF CHEMISTRY
Citation: Hong, D., Shin, K., James, M., & Tae, G. (2012). Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air-water interface. Soft Matter, 8(33), 8616-8623.
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. © 2012, Royal Society of Chemistry.
URI: http://dx.doi.org/10.1039/c2sm25885d
http://apo.ansto.gov.au/dspace/handle/10238/5450
ISSN: 1744-683X
Appears in Collections:Journal Articles

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