An amphipathic alpha-helical peptide from apolipoprotein A1 stabilizes protein polymer vesicles

L4F, an alpha helical peptide inspired by the lipid-binding domain of the ApoA1 protein, has potential applications in the reduction of inflammation involved with cardiovascular disease as well as an antioxidant effect that inhibits liver fibrosis. In addition to its biological activity, amphipathic...

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Veröffentlicht in:	Journal of controlled release 2014-10, Vol.191, p.15-23
Hauptverfasser:	Pastuszka, Martha K., Wang, Xiangdong, Lock, Lye Lin, Janib, Siti Mohd, Cui, Honggang, DeLeve, Laurie D., MacKay, J. Andrew
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Anti-Inflammatory Agents - administration & dosage Anti-Inflammatory Agents - blood Anti-Inflammatory Agents - chemistry Anti-Inflammatory Agents - pharmacokinetics Antioxidants - administration & dosage Antioxidants - chemistry Antioxidants - pharmacokinetics Apolipoprotein A-I - administration & dosage Apolipoprotein A-I - blood Apolipoprotein A-I - chemistry Apolipoprotein A-I - genetics Apolipoprotein A-I - pharmacokinetics Cells, Cultured Chemistry, Pharmaceutical Cryo-TEM Drug Carriers Elastin-like polypeptide Genetic Engineering Half-Life Hepatic Stellate Cells - drug effects Hepatic Stellate Cells - metabolism Hydrodynamic radius Injections, Intravenous L-4F Mice Nanoparticle Nanoparticles Nanotechnology Particle Size Peptide Fragments - administration & dosage Peptide Fragments - blood Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - pharmacokinetics Protein Stability Protein Structure, Secondary Rats Recombinant Fusion Proteins - chemistry Technology, Pharmaceutical - methods Tropoelastin - chemistry Tropoelastin - genetics Tropoelastin - metabolism Vesicle
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