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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Lipopeptide</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><p><b>Lipopeptide</b> sind <a href="Peptide" class="mw-redirect" title="Peptide">Peptide</a>, die mit <a href="Lipide" title="Lipide">Lipiden</a> modifiziert sind.<sup id="cite_ref-Hamley_1-0" class="reference"><a href="#cite_note-Hamley-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>
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<div class="mw-heading mw-heading2"><h2 id="Eigenschaften">Eigenschaften</h2></div>
<p>Typische <a href="Hydrophob" class="mw-redirect" title="Hydrophob">hydrophobe</a> Modifikationen an Peptiden sind z. B. die <a href="Palmitoylierung" title="Palmitoylierung">Palmitoylierung</a>, die <a href="Myristylierung" class="mw-redirect" title="Myristylierung">Myristylierung</a>, die <a href="Farnesylierung" title="Farnesylierung">Farnesylierung</a>, der <a href="GPI-Anker" title="GPI-Anker">GPI-Anker</a> und die <a href="Geranylgeranylierung" title="Geranylgeranylierung">Geranylgeranylierung</a>. Durch diese Modifikationen (<a href="Lipidanker" title="Lipidanker">Lipidanker</a>) binden Lipopeptide an <a href="Zellmembran" title="Zellmembran">Zellmembranen</a>. Daneben sind sie <a href="Amphiphil" class="mw-redirect" title="Amphiphil">amphiphil</a><sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> und lagern sich in wässrigen Lösungen oberhalb ihrer jeweiligen <a href="Kritische_Mizellbildungskonzentration" title="Kritische Mizellbildungskonzentration">kritischen Mizellbildungskonzentration</a> zusammen.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup>
</p><p>Manche Lipopeptide aktivieren die <a href="Angeborene_Immunantwort" title="Angeborene Immunantwort">angeborene Immunantwort</a> über die <a href="Toll-like_Receptor" class="mw-redirect" title="Toll-like Receptor">Toll-like Rezeptoren</a> 1, 2 und 6. Das <a href="CSK4-Motiv" title="CSK4-Motiv">CSK<sub>4</sub>-Motiv</a> mit einer bis drei Palmitoylierungen bindet an TLR.<sup id="cite_ref-Hamley_1-1" class="reference"><a href="#cite_note-Hamley-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>
</p><p>Die Analyse von Lipopeptiden erfolgt durch eine Form der <a href="Immunf%C3%A4rbung" class="mw-redirect" title="Immunfärbung">Immunfärbung</a> oder per <a href="Fl%C3%BCssigchromatographie_mit_Massenspektrometrie-Kopplung" title="Flüssigchromatographie mit Massenspektrometrie-Kopplung">LC-MS</a>.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>
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<div class="mw-heading mw-heading2"><h2 id="Anwendungen">Anwendungen</h2></div>
<p>Manche lineare<sup id="cite_ref-Hamley_1-2" class="reference"><a href="#cite_note-Hamley-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> oder <a href="Cyclopeptide" title="Cyclopeptide">zyklische</a><sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> Lipopeptide werden als <a href="Antibiotikum" title="Antibiotikum">Antibiotika</a> verwendet oder besitzen antibiotische Wirkungen, z. B. <a href="Daptomycin" title="Daptomycin">Daptomycin</a>, Bacillomycin, Echinocandine wie <a href="Caspofungin" title="Caspofungin">Caspofungin</a>, <a href="Jagaricin" title="Jagaricin">Jagaricin</a>, <a href="Malacidine" title="Malacidine">Malacidine</a>, Mycosubtilin, Iturin A,<sup id="cite_ref-Mnif_7-0" class="reference"><a href="#cite_note-Mnif-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Fengycin<sup id="cite_ref-Mnif_7-1" class="reference"><a href="#cite_note-Mnif-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> und <a href="Surfactin" title="Surfactin">Surfactin</a>.<sup id="cite_ref-Mnif_7-2" class="reference"><a href="#cite_note-Mnif-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Die antibiotische Wirkung der Lipopeptide basiert auf einem anderen Mechanismus als andere Antibiotika-Typen, bei dem eine <a href="Resistenz" title="Resistenz">Resistenzbildung</a> erschwert ist.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup>
</p><p>Weiterhin werden Lipopeptide zur Verwendung als <a href="Futtermittelzusatzstoff" title="Futtermittelzusatzstoff">Futtermittelzusatzstoff</a>, <a href="Chemotherapeutikum" title="Chemotherapeutikum">Chemotherapeutikum</a>, <a href="Thrombolytikum" class="mw-redirect" title="Thrombolytikum">Thrombolytikum</a> und als <a href="Einschlussimmobilisierung" title="Einschlussimmobilisierung">Vesikelbildner</a> untersucht.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Als Vesikelbildner werden z. B. das <a href="Zellpenetrierendes_Peptid" title="Zellpenetrierendes Peptid">zellpenetrierende Peptid</a> <i>TAT<sub>48–60</sub></i> mit ein bis vier <a href="Alkylgruppe" title="Alkylgruppe">Alkylgruppen</a><sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> oder palmitoyliertes <a href="Alanin" title="Alanin">Ala</a>‐<a href="Glycin" title="Glycin">Gly</a>‐<a href="Phenylalanin" title="Phenylalanin">Phe</a>‐<a href="Leucin" title="Leucin">Leu</a>‐<a href="Arginin" title="Arginin">Arg</a> verwendet.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Das Lipopeptid Palmitoyl-<a href="Lysin" title="Lysin">Lys</a>‐<a href="Threonin" title="Threonin">Thr</a>‐Thr‐Lys‐<a href="Serin" title="Serin">Ser</a> (kurz: C16-KTTKS) wird zur Glättung von Mimikfalten verwendet (Handelsname <i>Matrikine</i>).<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> Bestimmte Lipopeptide (<a href="Pepducine" title="Pepducine">Pepducine</a>) werden zur Modulation von <a href="G-Protein" class="mw-redirect" title="G-Protein">G-Proteinen</a> untersucht.
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<div class="mw-heading mw-heading2"><h2 id="Weblinks">Weblinks</h2></div>
<div class="sisterproject" style="margin:0.1em 0 0 0;"><div class="noresize noviewer" style="display:inline-block; line-height:10px; min-width:1.6em; text-align:center;" aria-hidden="true" role="presentation"><span class="mw-default-size" typeof="mw:File"><span title="Commons"></span></span></div><b><span class=""><a class="external text" href="https://commons.wikimedia.org/wiki/Category:Lipopeptides?uselang=de"><span lang="en">Commons</span>: Lipopeptide</a></span></b> – Sammlung von Bildern, Videos und Audiodateien</div>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-Hamley-1"><span class="mw-cite-backlink">↑ <sup><a href="#cite_ref-Hamley_1-0">a</a></sup> <sup><a href="#cite_ref-Hamley_1-1">b</a></sup> <sup><a href="#cite_ref-Hamley_1-2">c</a></sup></span> <span class="reference-text">Ian W. Hamley: <i>Lipopeptides: from self-assembly to bioactivity.</i> In: <i><a href="Chemical_Communications" title="Chemical Communications">Chemical Communications</a>.</i> 51, 2015, S. 8574, <a href="https://doi.org/10.1039/c5cc01535a" class="extiw external" title="doi:10.1039/c5cc01535a">doi:10.1039/c5cc01535a</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/25797909?dopt=Abstract">PMID 25797909</a>.</span>
</li>
<li id="cite_note-2"><span class="mw-cite-backlink"><a href="#cite_ref-2">↑</a></span> <span class="reference-text">T. Schneider, A. Müller, H. Miess, H. Gross: <i>Cyclic lipopeptides as antibacterial agents – potent antibiotic activity mediated by intriguing mode of actions.</i> In: <i><a href="International_Journal_of_Medical_Microbiology" title="International Journal of Medical Microbiology">International Journal of Medical Microbiology</a>.</i> Band 304, Nummer 1, Januar 2014, S. 37–43, <a href="https://doi.org/10.1016/j.ijmm.2013.08.009" class="extiw external" title="doi:10.1016/j.ijmm.2013.08.009">doi:10.1016/j.ijmm.2013.08.009</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/24119568?dopt=Abstract">PMID 24119568</a>.</span>
</li>
<li id="cite_note-3"><span class="mw-cite-backlink"><a href="#cite_ref-3">↑</a></span> <span class="reference-text">J. A. Hutchinson, S. Burholt, I. W. Hamley: <i>Peptide hormones and lipopeptides: from self-assembly to therapeutic applications.</i> In: <i><a href="Journal_of_Peptide_Science" title="Journal of Peptide Science">Journal of Peptide Science</a>.</i> Band 23, Nummer 2, Februar 2017, S. 82–94, <a href="https://doi.org/10.1002/psc.2954" class="extiw external" title="doi:10.1002/psc.2954">doi:10.1002/psc.2954</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/28127868?dopt=Abstract">PMID 28127868</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5324658/">PMC 5324658</a> (freier Volltext).</span>
</li>
<li id="cite_note-4"><span class="mw-cite-backlink"><a href="#cite_ref-4">↑</a></span> <span class="reference-text">J. Zemenová, D. Sýkora, L. Maletínská, J. Kuneš: <i>Lipopeptides as therapeutics: applications and in vivo quantitative analysis.</i> In: <i><a href="Bioanalysis" title="Bioanalysis">Bioanalysis</a>.</i> Band 9, Nummer 2, Januar 2017, S. 215–230, <a href="https://doi.org/10.4155/bio-2016-0206" class="extiw external" title="doi:10.4155/bio-2016-0206">doi:10.4155/bio-2016-0206</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/27960546?dopt=Abstract">PMID 27960546</a>.</span>
</li>
<li id="cite_note-5"><span class="mw-cite-backlink"><a href="#cite_ref-5">↑</a></span> <span class="reference-text">S. Patel, S. Ahmed, J. S. Eswari: <i>Therapeutic cyclic lipopeptides mining from microbes: latest strides and hurdles.</i> In: <i>World Journal of Microbiology & Biotechnology.</i> Band 31, Nummer 8, August 2015, S. 1177–1193, <a href="https://doi.org/10.1007/s11274-015-1880-8" class="extiw external" title="doi:10.1007/s11274-015-1880-8">doi:10.1007/s11274-015-1880-8</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/26041368?dopt=Abstract">PMID 26041368</a>.</span>
</li>
<li id="cite_note-6"><span class="mw-cite-backlink"><a href="#cite_ref-6">↑</a></span> <span class="reference-text">T. Schneider, A. Müller, H. Miess, H. Gross: <i>Cyclic lipopeptides as antibacterial agents – potent antibiotic activity mediated by intriguing mode of actions.</i> In: <i>International Journal of Medical Microbiology.</i> Band 304, Nummer 1, Januar 2014, S. 37–43, <a href="https://doi.org/10.1016/j.ijmm.2013.08.009" class="extiw external" title="doi:10.1016/j.ijmm.2013.08.009">doi:10.1016/j.ijmm.2013.08.009</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/24119568?dopt=Abstract">PMID 24119568</a>.</span>
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<li id="cite_note-Mnif-7"><span class="mw-cite-backlink">↑ <sup><a href="#cite_ref-Mnif_7-0">a</a></sup> <sup><a href="#cite_ref-Mnif_7-1">b</a></sup> <sup><a href="#cite_ref-Mnif_7-2">c</a></sup></span> <span class="reference-text">I. Mnif, D. Ghribi: <i>Review lipopeptides biosurfactants: Mean classes and new insights for industrial, biomedical, and environmental applications.</i> In: <i>Biopolymers.</i> Band 104, Nummer 3, Mai 2015, S. 129–147, <a href="https://doi.org/10.1002/bip.22630" class="extiw external" title="doi:10.1002/bip.22630">doi:10.1002/bip.22630</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/25808118?dopt=Abstract">PMID 25808118</a>.</span>
</li>
<li id="cite_note-8"><span class="mw-cite-backlink"><a href="#cite_ref-8">↑</a></span> <span class="reference-text">J. J. Koh, S. Lin, R. W. Beuerman, S. Liu: <i>Recent advances in synthetic lipopeptides as anti-microbial agents: designs and synthetic approaches.</i> In: <i>Amino Acids.</i> Band 49, Nummer 10, Oktober 2017, S. 1653–1677, <a href="https://doi.org/10.1007/s00726-017-2476-4" class="extiw external" title="doi:10.1007/s00726-017-2476-4">doi:10.1007/s00726-017-2476-4</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/28823054?dopt=Abstract">PMID 28823054</a>.</span>
</li>
<li id="cite_note-9"><span class="mw-cite-backlink"><a href="#cite_ref-9">↑</a></span> <span class="reference-text">H. Zhao, D. Shao, C. Jiang, J. Shi, Q. Li, Q. Huang, M. S. Rajoka, H. Yang, M. Jin: <i>Biological activity of lipopeptides from Bacillus.</i> In: <i><a href="Applied_Microbiology_and_Biotechnology" title="Applied Microbiology and Biotechnology">Applied Microbiology and Biotechnology</a>.</i> Band 101, Nummer 15, August 2017, S. 5951–5960, <a href="https://doi.org/10.1007/s00253-017-8396-0" class="extiw external" title="doi:10.1007/s00253-017-8396-0">doi:10.1007/s00253-017-8396-0</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/28685194?dopt=Abstract">PMID 28685194</a>.</span>
</li>
<li id="cite_note-10"><span class="mw-cite-backlink"><a href="#cite_ref-10">↑</a></span> <span class="reference-text">P. Zhang, A. G. Cheetham, Y. A. Lin, H. Cui: <i>Self-assembled Tat nanofibers as effective drug carrier and transporter.</i> In: <i><a href="ACS_Nano" title="ACS Nano">ACS Nano</a>.</i> Band 7, Nummer 7, Juli 2013, S. 5965–5977, <a href="https://doi.org/10.1021/nn401667z" class="extiw external" title="doi:10.1021/nn401667z">doi:10.1021/nn401667z</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23758167?dopt=Abstract">PMID 23758167</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3799919/">PMC 3799919</a> (freier Volltext).</span>
</li>
<li id="cite_note-11"><span class="mw-cite-backlink"><a href="#cite_ref-11">↑</a></span> <span class="reference-text">M. Mazza, R. Notman, J. Anwar, A. Rodger, M. Hicks, G. Parkinson, D. McCarthy, T. Daviter, J. Moger, N. Garrett, T. Mead, M. Briggs, A. G. Schätzlein, I. F. Uchegbu: <i>Nanofiber-based delivery of therapeutic peptides to the brain.</i> In: <i>ACS Nano.</i> Band 7, Nummer 2, Februar 2013, S. 1016–1026, <a href="https://doi.org/10.1021/nn305193d" class="extiw external" title="doi:10.1021/nn305193d">doi:10.1021/nn305193d</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23289352?dopt=Abstract">PMID 23289352</a>.</span>
</li>
<li id="cite_note-12"><span class="mw-cite-backlink"><a href="#cite_ref-12">↑</a></span> <span class="reference-text">V. Castelletto, I. W. Hamley, J. Perez, L. Abezgauz, D. Danino: <i>Fibrillar superstructure from extended nanotapes formed by a collagen-stimulating peptide.</i> In: <i>Chemical Communications.</i> Band 46, Nummer 48, Dezember 2010, S. 9185–9187, <a href="https://doi.org/10.1039/c0cc03793a" class="extiw external" title="doi:10.1039/c0cc03793a">doi:10.1039/c0cc03793a</a>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/21031196?dopt=Abstract">PMID 21031196</a>.</span>
</li>
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