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Sequence and length optimization of membrane active coiled coils for triggered liposome release
Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0002-9481-8828
Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0002-1781-1489
Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0001-7921-8915
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2019 (English)In: Biochimica et Biophysica Acta - Biomembranes, ISSN 0005-2736, E-ISSN 1879-2642, Vol. 1862, no 2, p. 449-456Article in journal (Refereed) Published
Abstract [en]

Defined and tunable peptide-lipid membrane interactions that trigger the release of liposome encapsulated drugs may offer a route to improving the efficiency and specificity of liposome-based drug delivery systems, but this require means to tailor the performance of the membrane active peptides. In this paper, the membrane activity of a de novo designed coiled coil peptide has been optimized with respect to sequence and size to improve release efficiency of liposome encapsulated cargo. The peptides were only membrane active when covalently conjugated to the liposomes. Two amino acid substitutions were made to enhance the amphipathic characteristics of the peptide, which increased the release by a factor of five at 1 mu M. Moreover, the effect of peptide length was investigated by varying the number of heptad repeats from 2 to 5, yielding the peptides KVC2-KVC5. The shortest peptide (KVC2) showed the least interaction with the membrane and proved less efficient than the longer peptides in releasing the liposomal cargo. The peptide with three heptads (KVC3) caused liposome aggregation whereas KVC4 proved to effectively release the liposomal cargo without causing aggregation. The longest peptide (KVC5) demonstrated the most defined a-helical secondary structure and the highest liposome surface concentration but showed slower release kinetics than KVC4. The four heptad peptide KVC4 consequently displayed optimal properties for triggering the release and is an interesting candidate for further development of bioresponsive and tunable liposomal drug delivery systems.

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV , 2019. Vol. 1862, no 2, p. 449-456
Keywords [en]
Liposome; Membrane active peptide; Coiled coil; Folding; Drug delivery
National Category
Pharmaceutical Sciences
Identifiers
URN: urn:nbn:se:liu:diva-154673DOI: 10.1016/j.bbamem.2018.11.005ISI: 000456764100010PubMedID: 30423325OAI: oai:DiVA.org:liu-154673DiVA, id: diva2:1292871
Note

Funding Agencies|Swedish Research Council (VR) [2017-04475]; Swedish Cancer Foundation [CAN 2017/430]; Swedish Government Strategic Research Area in Materials Science on Functional Materials at Linkoping University [2009-00971]

Available from: 2019-03-01 Created: 2019-03-01 Last updated: 2019-03-26

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The full text will be freely available from 2019-11-10 15:19
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Skyttner, CamillaSelegård, RobertLarsson, JakobAronsson, ChristopherEnander, KarinAili, Daniel
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