Oxime ether lipids containing hydroxylated head groups are more superior siRNA delivery agents than their nonhydroxylated counterparts

To evaluate the structure-activity relationship of oxime ether lipids (OELs) containing modifications in the hydrophobic domains (chain length, degree of unsaturation) and hydrophilic head groups (polar domain hydroxyl groups) toward complex formation with siRNA molecules and siRNA delivery efficien...

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Bibliographic Details
Published in:Nanomedicine (London, England) England), 2015-09, Vol.10 (18), p.2805-2818
Main Authors: Gupta, Kshitij, Mattingly, Stephanie J, Knipp, Ralph J, Afonin, Kirill A, Viard, Mathias, Bergman, Joseph T, Stepler, Marissa, Nantz, Michael H, Puri, Anu, Shapiro, Bruce A
Format: Article
Language:English
Subjects:
breast cancer cells
Breast Neoplasms - genetics
Cell Line, Tumor
Ethers - chemistry
Female
Green Fluorescent Proteins - genetics
Humans
Hydroxylation
Lipids
Lipids - chemistry
lipoplexes
Liposomes - chemistry
Methods
nonsymmetric hydrophobic domain
oxime ether lipids
Oximes - chemistry
Pharmacological research
Properties
RNA Interference
RNA, Small Interfering - administration & dosage
RNA, Small Interfering - genetics
structure-activity relationship
Structure-activity relationships (Biochemistry)
Transfection - methods
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Summary:To evaluate the structure-activity relationship of oxime ether lipids (OELs) containing modifications in the hydrophobic domains (chain length, degree of unsaturation) and hydrophilic head groups (polar domain hydroxyl groups) toward complex formation with siRNA molecules and siRNA delivery efficiency of resulting complexes to a human breast cancer cell line (MDA-MB-231). Ability of lipoplex formation between oxime ether lipids with nucleic acids were examined using biophysical techniques. The potential of OELs to deliver nucleic acids and silence green fluorescent protein (GFP) gene was analyzed using MDA-MB-231 and MDA-MB-231/GFP cells, respectively. : Introduction of hydroxyl groups to the polar domain of the OELs and unsaturation into the hydrophobic domain favor higher transfection and gene silencing in a cell culture system.
ISSN:1743-5889
1748-6963
1748-6963
DOI:10.2217/nnm.15.105