Modification of a Designed Amphipathic Cell-Penetrating Peptide and Its Effect on Solubility, Secondary Structure, and Uptake Efficiency
The development of safe and efficient nonviral gene delivery carriers has received a great deal of attention in the past decade. A class of amphipathic peptides has shown to be able to cross cell membranes and deliver cargo to the intracellular environment. Here, we introduce an 18-mer amphipathic p...
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| Veröffentlicht in: | Biochemistry (Easton) 2013-05, Vol.52 (20), p.3428-3435 |
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| creator | Jafari, Mousa Karunaratne, D. Nedra Sweeting, Chad M Chen, P |
| description | The development of safe and efficient nonviral gene delivery carriers has received a great deal of attention in the past decade. A class of amphipathic peptides has shown to be able to cross cell membranes and deliver cargo to the intracellular environment. Here, we introduce an 18-mer amphipathic peptide, C6M1, as a modified version of peptide C6 for short interfering RNA (siRNA) delivery. The importance of tryptophan residues and the effect of peptide sequence modification on its solubility, secondary structure, cytotoxicity, and uptake efficiency were investigated. The solubility of C6M1 in aqueous solutions was greatly enhanced compared to that of C6, confirmed by surface tension and anilinonaphthalene-8-sulfonic acid fluorescence measurements. C6M1 had a random/helical structure in water with the ability to attain a helical conformation in the presence of anionic components or membrane-mimicking environments. The modification significantly reduced the cytotoxicity of the peptide, making it a safer carrier for siRNA delivery. C6M1 was also found ∼90% more efficient than C6 in delivering Cy3-labeled siRNA in Chinese hamster ovary cells. |
| doi_str_mv | 10.1021/bi4001326 |
| format | Article |
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The solubility of C6M1 in aqueous solutions was greatly enhanced compared to that of C6, confirmed by surface tension and anilinonaphthalene-8-sulfonic acid fluorescence measurements. C6M1 had a random/helical structure in water with the ability to attain a helical conformation in the presence of anionic components or membrane-mimicking environments. The modification significantly reduced the cytotoxicity of the peptide, making it a safer carrier for siRNA delivery. C6M1 was also found ∼90% more efficient than C6 in delivering Cy3-labeled siRNA in Chinese hamster ovary cells.</description><subject>Animals</subject><subject>Cell-Penetrating Peptides - chemistry</subject><subject>Cell-Penetrating Peptides - metabolism</subject><subject>CHO Cells</subject><subject>Circular Dichroism</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Mesylates - chemistry</subject><subject>Mesylates - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>RNA, Small Interfering - chemistry</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Solubility</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Surface Tension</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1uEzEUhS0EomlhwQtU3iBRqQP-z8wyCgUiBVEpdD3y2Net24k92J5F3oDHxiWlK1ZXV_rOkc6H0DtKPlLC6KfBC0IoZ-oFWlDJSCO6Tr5EC0KIalinyAk6zfm-voIsxWt0wriiYtm2C_T7e7TeeaOLjwFHhzX-DNnfBrB4tZ_u_KTLnTd4DePYXEOAkioabvE1TMVbwDpYvCkZXzkHpuBasovjPPjRl8Ml3oGJwep0wLuSZlPmBJd_IzdT0Q_wmPLGQzCHN-iV02OGt0_3DN18ufq5_tZsf3zdrFfbRnMqS8Nop5eWtKrjgpFWM2I6yVrJOSOiY5Q7p4m0rXKcQSvtQIXQQ3XitJWWKX6GPhx7pxR_zZBLv_fZ1HU6QJxzT4WSrVKK84peHFGTYs4JXD8lv69jekr6R_H9s_jKnj_VzsMe7DP5z3QF3h8BbXJ_H-cU6sr_FP0BGTOI2A</recordid><startdate>20130521</startdate><enddate>20130521</enddate><creator>Jafari, Mousa</creator><creator>Karunaratne, D. 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| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Cell-Penetrating Peptides - chemistry Cell-Penetrating Peptides - metabolism CHO Cells Circular Dichroism Cricetinae Cricetulus Mesylates - chemistry Mesylates - metabolism Protein Structure, Secondary RNA, Small Interfering - chemistry RNA, Small Interfering - metabolism Solubility Spectroscopy, Fourier Transform Infrared Surface Tension |
| title | Modification of a Designed Amphipathic Cell-Penetrating Peptide and Its Effect on Solubility, Secondary Structure, and Uptake Efficiency |
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