Effects of Side Chain Configuration and Backbone Spacing on the Gene Delivery Properties of Lysine-Derived Cationic Polymers
Identifieur interne : 002F38 ( Main/Exploration ); précédent : 002F37; suivant : 002F39Effects of Side Chain Configuration and Backbone Spacing on the Gene Delivery Properties of Lysine-Derived Cationic Polymers
Auteurs : Sarah E. Eldred [États-Unis] ; Margaret R. Pancost [États-Unis] ; Karin M. Otte [États-Unis] ; David Rozema [États-Unis, Oman] ; Shannon S. Stahl [États-Unis, Oman] ; Samuel H. Gellman [États-Unis, Oman]Source :
- Bioconjugate Chemistry [ 1043-1802 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- administration et posologie : ADN.
- génétique : ADN.
- pharmacologie : Chloroquine, Transfection.
- Animaux, Cations, Humains, Lignée cellulaire, Lysine, Polymères, Structure moléculaire, Transfection.
English descriptors
- KwdEn :
- MESH :
- chemical , administration & dosage : DNA.
- chemical , chemistry : Cations, Lysine, Polymers.
- chemical , genetics : DNA.
- chemical , pharmacology : Chloroquine.
- instrumentation : Transfection.
- methods : Transfection.
- Animals, Cell Line, Chlorocebus aethiops, Humans, Molecular Structure.
Abstract
A series of lysine-based oligomers (18 residues) that differ in side chain configuration or side chain spacing along the backbone was tested for DNA transfection activity. Although materials constructed from lysine are not the most effective polymeric transfection agents, we have chosen l-lysine-based molecules as a starting point because this system allows us to examine the functional effects of incremental changes in polycation structure. The oligomer constructed from β3-homolysine (β3-hLys) and that from α-d-lysine were superior to an α-l-lysine 18-mer in gene delivery assays. This improved activity is attributed to the fact that the α-l-peptide is a protease substrate while the other 18-mers are not. This conclusion is supported by the effects of chloroquine on transfection activity, based on the protease inhibition activity of chloroquine. To our knowledge, these results represent the first direct comparison of a d-lysine oligomer with an l-lysine oligomer in the context of gene delivery. Poly(β3-hLys) was synthesized from the ring opening polymerization of the corresponding lactam. The DNA transfection ability of this polymer was compared with that of commercially available poly(l-lysine) (PLL). In each case the polymer was more active than the corresponding oligomer.
Url:
DOI: 10.1021/bc050017c
Affiliations:
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Gene Delivery Properties of Lysine-Derived Cationic Polymers</title><author><name sortKey="Eldred, Sarah E" sort="Eldred, Sarah E" uniqKey="Eldred S" first="Sarah E." last="Eldred">Sarah E. Eldred</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Pancost, Margaret R" sort="Pancost, Margaret R" uniqKey="Pancost M" first="Margaret R." last="Pancost">Margaret R. Pancost</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Otte, Karin M" sort="Otte, Karin M" uniqKey="Otte K" first="Karin M." last="Otte">Karin M. Otte</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Rozema, David" sort="Rozema, David" uniqKey="Rozema D" first="David" last="Rozema">David Rozema</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation><affiliation wicri:level="4"><country wicri:rule="url">Oman</country><wicri:regionArea> To whom correspondence should be addressed. E-mailaddresses: stahl@chem.wisc.edu, gellman@chem.wisc.edu</wicri:regionArea><wicri:noRegion>gellman@chem.wisc.edu</wicri:noRegion></affiliation></author><author><name sortKey="Stahl, Shannon S" sort="Stahl, Shannon S" uniqKey="Stahl S" first="Shannon S." last="Stahl">Shannon S. Stahl</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation><affiliation wicri:level="4"><country wicri:rule="url">Oman</country><wicri:regionArea> To whom correspondence should be addressed. E-mailaddresses: stahl@chem.wisc.edu, gellman@chem.wisc.edu</wicri:regionArea><wicri:noRegion>gellman@chem.wisc.edu</wicri:noRegion></affiliation></author><author><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H." last="Gellman">Samuel H. Gellman</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Department of Chemistry, University of WisconsinMadison, 1101 University Ave., Madison, Wisconsin 53706,and Mirus Corporation, 505 S. Rosa Road, Madison</wicri:cityArea></affiliation><affiliation></affiliation><affiliation wicri:level="4"><country wicri:rule="url">Oman</country><wicri:regionArea> To whom correspondence should be addressed. E-mailaddresses: stahl@chem.wisc.edu, gellman@chem.wisc.edu</wicri:regionArea><wicri:noRegion>gellman@chem.wisc.edu</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Bioconjugate Chemistry</title><title level="j" type="abbrev">Bioconjugate Chem.</title><idno type="ISSN">1043-1802</idno><idno type="eISSN">1520-4812</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">2005</date><date type="published">2005</date><biblScope unit="vol">16</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="694">694</biblScope><biblScope unit="page" to="699">699</biblScope></imprint><idno type="ISSN">1043-1802</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1043-1802</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cations (chemistry)</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Chloroquine (pharmacology)</term><term>DNA (administration & dosage)</term><term>DNA (genetics)</term><term>Humans</term><term>Lysine (chemistry)</term><term>Molecular Structure</term><term>Polymers (chemistry)</term><term>Transfection (instrumentation)</term><term>Transfection (methods)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (administration et posologie)</term><term>ADN (génétique)</term><term>Animaux</term><term>Cations ()</term><term>Chloroquine (pharmacologie)</term><term>Humains</term><term>Lignée cellulaire</term><term>Lysine ()</term><term>Polymères ()</term><term>Structure moléculaire</term><term>Transfection ()</term><term>Transfection (instrumentation)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cations</term><term>Lysine</term><term>Polymers</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chloroquine</term></keywords><keywords scheme="MESH" qualifier="administration et posologie" xml:lang="fr"><term>ADN</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Transfection</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Transfection</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Chloroquine</term><term>Transfection</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Molecular Structure</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cations</term><term>Humains</term><term>Lignée cellulaire</term><term>Lysine</term><term>Polymères</term><term>Structure moléculaire</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract">A series of lysine-based oligomers (18 residues) that differ in side chain configuration or side chain spacing along the backbone was tested for DNA transfection activity. Although materials constructed from lysine are not the most effective polymeric transfection agents, we have chosen l-lysine-based molecules as a starting point because this system allows us to examine the functional effects of incremental changes in polycation structure. The oligomer constructed from β3-homolysine (β3-hLys) and that from α-d-lysine were superior to an α-l-lysine 18-mer in gene delivery assays. This improved activity is attributed to the fact that the α-l-peptide is a protease substrate while the other 18-mers are not. This conclusion is supported by the effects of chloroquine on transfection activity, based on the protease inhibition activity of chloroquine. To our knowledge, these results represent the first direct comparison of a d-lysine oligomer with an l-lysine oligomer in the context of gene delivery. Poly(β3-hLys) was synthesized from the ring opening polymerization of the corresponding lactam. The DNA transfection ability of this polymer was compared with that of commercially available poly(l-lysine) (PLL). In each case the polymer was more active than the corresponding oligomer.</div></front></TEI><affiliations><list><country><li>Oman</li><li>États-Unis</li></country><region><li>Wisconsin</li></region></list><tree><country name="États-Unis"><region name="Wisconsin"><name sortKey="Eldred, Sarah E" sort="Eldred, Sarah E" uniqKey="Eldred S" first="Sarah E." last="Eldred">Sarah E. Eldred</name></region><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H." last="Gellman">Samuel H. Gellman</name><name sortKey="Otte, Karin M" sort="Otte, Karin M" uniqKey="Otte K" first="Karin M." last="Otte">Karin M. Otte</name><name sortKey="Pancost, Margaret R" sort="Pancost, Margaret R" uniqKey="Pancost M" first="Margaret R." last="Pancost">Margaret R. Pancost</name><name sortKey="Rozema, David" sort="Rozema, David" uniqKey="Rozema D" first="David" last="Rozema">David Rozema</name><name sortKey="Stahl, Shannon S" sort="Stahl, Shannon S" uniqKey="Stahl S" first="Shannon S." last="Stahl">Shannon S. Stahl</name></country><country name="Oman"><noRegion><name sortKey="Rozema, David" sort="Rozema, David" uniqKey="Rozema D" first="David" last="Rozema">David Rozema</name></noRegion><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H." last="Gellman">Samuel H. Gellman</name><name sortKey="Stahl, Shannon S" sort="Stahl, Shannon S" uniqKey="Stahl S" first="Shannon S." last="Stahl">Shannon S. Stahl</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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