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Open AccessArticle

Interaction of a Polyarginine Peptide with Membranes of Different Mechanical Properties

1
Facultad de Ciencias Químicas, Departamento de Química Biológica Ranwel Caputto, Universidad Nacional de Córdoba, X5000HUA Córdoba, Argentina
2
Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), CONICET, Universidad Nacional de Córdoba, X5000HUA Córdoba, Argentina
3
ICB-CONICET & Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Cuyo, M5502JMA Mendoza, Argentina
4
Facultad de Ciencias Químicas, Departamento de Fisicoquímica, Universidad Nacional de Cordoba, X5000HUA Córdoba, Argentina
5
Consejo Nacional de Investigaciones Científicas y Tecnicas, CONICET, Instituto de Investigaciones en Fisicoquímica de Córdoba, INFIQC, X5000HUA Córdoba, Argentina
6
Instituto de Investigación Médica Mercedes y Martín Ferreyra (INIMEC-CONICET-Universidad Nacional de Córdoba), X5016NST Córdoba, Argentina
*
Author to whom correspondence should be addressed.
Biomolecules 2019, 9(10), 625; https://doi.org/10.3390/biom9100625
Received: 26 September 2019 / Revised: 15 October 2019 / Accepted: 17 October 2019 / Published: 18 October 2019
The membrane translocation efficiency of cell penetrating peptides (CPPs) has been largely studied, and poly-arginines have been highlighted as particularly active CPPs, especially upon negatively charged membranes. Here we inquire about the influence of membrane mechanical properties in poly-arginine adsorption, penetration and translocation, as well as the subsequent effect on the host membrane. For this, we selected anionic membranes exhibiting different rigidity and fluidity, and exposed them to the nona-arginine KR9C. Three different membrane compositions were investigated, all of them having 50% of the anionic lipid 1,2-dioleoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (DOPG), thus, ensuring a high affinity of the peptide for membrane surfaces. The remaining 50% was a saturated PC (1,2-dipalmitoyl-sn-glycero-3-phosphocholine, DPPC), an unsaturated PC (1,2-dioleoyl-sn-glycero-3-phosphocholine, DOPC) or a mixture of DOPC with cholesterol. Peptide-membrane interactions were studied using four complementary models for membranes: Langmuir monolayers, Large Unilamellar Vesicles, Black Lipid Membranes and Giant Unilamellar Vesicles. The patterns of interaction of KR9C varied within the different membrane compositions. The peptide strongly adsorbed on membranes with cholesterol, but did not incorporate or translocate them. KR9C stabilized phase segregation in DPPC/DOPG films and promoted vesicle rupture. DOPC/DOPG appeared like the better host for peptide translocation: KR9C adsorbed, inserted and translocated these membranes without breaking them, despite softening was observed. View Full-Text
Keywords: cell penetration peptides; liquid-ordered phase; membrane heterogeneities; membrane rheology cell penetration peptides; liquid-ordered phase; membrane heterogeneities; membrane rheology
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MDPI and ACS Style

Crosio, M.A.; Via, M.A.; Cámara, C.I.; Mangiarotti, A.; Del Pópolo, M.G.; Wilke, N. Interaction of a Polyarginine Peptide with Membranes of Different Mechanical Properties. Biomolecules 2019, 9, 625.

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