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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Tripeptide</span></h1>
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<p><b>Tripeptide</b> sind aus drei <a href="Aminos%C3%A4ure" class="mw-redirect" title="Aminosäure">Aminosäure</a>-Resten aufgebaute <a href="Peptide" class="mw-redirect" title="Peptide">Peptide</a> und zählen zur Gruppe der <a href="Oligopeptide" title="Oligopeptide">Oligopeptide</a>. Wie andere Oligopeptide besitzen Tripeptide häufig eine sehr spezifische physiologische Wirkung, z. B. in der <a href="Neurochemie" title="Neurochemie">Neurochemie</a>, im <a href="Stoffwechsel" title="Stoffwechsel">Stoffwechsel</a> und als <a href="Releasing-Hormon" class="mw-redirect" title="Releasing-Hormon">Releasing-Hormone</a>.<sup id="cite_ref-Römpp_2-0" class="reference"><a href="#cite_note-Römpp-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> <a href="Protein" title="Protein">Proteine</a> werden im Zuge der <a href="Verdauung" title="Verdauung">Verdauung</a> durch <a href="Peptidase" class="mw-redirect" title="Peptidase">Peptidasen</a> in Aminosäuren, <a href="Dipeptide" title="Dipeptide">Dipeptide</a> und Tripeptide zerlegt.<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> Tripeptide werden im <a href="D%C3%BCnndarm" title="Dünndarm">Dünndarm</a> und der <a href="Niere" title="Niere">Niere</a> über den <a href="Peptidtransporter_1" title="Peptidtransporter 1">Peptidtransporter 1</a> aufgenommen.<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> <a href="Tripeptidyl-Peptidase" class="mw-redirect" title="Tripeptidyl-Peptidase">Tripeptidyl-Peptidasen</a> sind Peptidasen, die Tripeptide abspalten.
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<div class="mw-heading mw-heading2"><h2 id="Beispiele">Beispiele</h2></div>
<p>Beispiele für natürlich vorkommende Tripeptide sind unter anderem die <a href="Antioxidans" title="Antioxidans">Antioxidantien</a> <a href="Glutathion" title="Glutathion">Glutathion</a>, die <a href="Ophthalmins%C3%A4ure" title="Ophthalminsäure">Ophthalminsäure</a>, den <a href="Proteaseinhibitor" class="mw-redirect" title="Proteaseinhibitor">Proteaseinhibitor</a> Leupeptin, das <a href="Melanotropin-Release-Inhibiting-Hormon" title="Melanotropin-Release-Inhibiting-Hormon">Melanotropin-Release-Inhibiting-Hormon</a>, die Lactotripeptide, GHK-Cu und das <a href="Herbizid" title="Herbizid">Herbizid</a> <a href="Bialaphos" title="Bialaphos">Bialaphos</a>. Einige natürliche Tripeptide besitzen eine <a href="Amidgruppe" class="mw-redirect" title="Amidgruppe">Amidgruppe</a> am <a href="C-Terminus" title="C-Terminus"><i>C</i>-Terminus</a>, wie <a href="Thyreoliberin" title="Thyreoliberin">Thyreoliberin</a> und das Melanotropin-Release-Inhibiting-Hormon. Die Peptidalkaloide unter den <a href="Mutterkornalkaloide" title="Mutterkornalkaloide">Mutterkornalkaloiden</a> enthalten unter anderem ein Tripeptid. Ein <a href="Nichtribosomales_Peptid" title="Nichtribosomales Peptid">nichtribosomal</a> erzeugtes Peptid ist das ACV-Tripeptid. Synthetische Tripeptide sind die <a href="ACE-Hemmer" title="ACE-Hemmer">ACE-Hemmer</a> <a href="Lisinopril" title="Lisinopril">Lisinopril</a>, <a href="Enalapril" title="Enalapril">Enalapril</a> und <a href="Ramipril" title="Ramipril">Ramipril</a> sowie <a href="Neuroprotektiv" class="mw-redirect" title="Neuroprotektiv">neuroprotektive</a> <a href="Analogon_(Chemie)" title="Analogon (Chemie)">Analoga</a> des Thyreoliberins.<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>
</p><p>Natürliche Tripeptide aus Milch (<a href="Casein" class="mw-redirect" title="Casein">Casein</a>) werden intakt resorbiert und wirken u. a. als schwache ACE-Hemmer.<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><sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Eine Wirkung an Opioidrezeptoren wird für Beta-<a href="Casomorphin" title="Casomorphin">Casomorphin</a> beschrieben.<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>
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<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>
<ul><li>S. Santos, I. Torcato, M. A. Castanho: <cite class="lang" lang="en" dir="auto" style="font-style:italic">Biomedical applications of dipeptides and tripeptides</cite>. In: <cite class="lang" lang="en" dir="auto" style="font-style:italic">Biopolymers</cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>98</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>4</span>, 2012, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>288–293</span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23193593?dopt=Abstract">PMID 23193593</a> (englisch).<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Tripeptide&rft.atitle=Biomedical+applications+of+dipeptides+and+tripeptides&rft.au=S.+Santos%2C+I.+Torcato%2C+M.+A.+Castanho&rft.date=2012&rft.genre=journal&rft.issue=4&rft.jtitle=Biopolymers&rft.pages=288-293&rft.pmid=23193593&rft.volume=98" style="display:none"> </span></li></ul>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<div class="mw-references-wrap"><ol class="references">
<li id="cite_note-rothe-1"><span class="mw-cite-backlink"><a href="#cite_ref-rothe_1-0">↑</a></span> <span class="reference-text">M. Rothe, K.-D. Steffen, I. Rothe: Synthese von Cyclo-tri-L-prolyl, einem Cyclo-tri-peptid mit neungliedrigem Ring, <a href="Angewandte_Chemie_(Zeitschrift)" title="Angewandte Chemie (Zeitschrift)">Angewandte Chemie</a> 77, 1965, S. 347–348.</span>
</li>
<li id="cite_note-Römpp-2"><span class="mw-cite-backlink"><a href="#cite_ref-Römpp_2-0">↑</a></span> <span class="reference-text"><a href="Otto-Albrecht_Neum%C3%BCller" title="Otto-Albrecht Neumüller">Otto-Albrecht Neumüller</a> (Hrsg.): <a href="R%C3%B6mpp_Lexikon_Chemie" title="Römpp Lexikon Chemie"><i>Römpps Chemie-Lexikon.</i></a> Band 6: <i>T–Z.</i> 8. neubearbeitete und erweiterte Auflage. Franckh’sche Verlagshandlung, Stuttgart 1988, ISBN 3-440-04516-1, S. 4360.</span>
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<li id="cite_note-3"><span class="mw-cite-backlink"><a href="#cite_ref-3">↑</a></span> <span class="reference-text">G. Wu: <i>Dietary protein intake and human health.</i> In: <i>Food & function.</i> Band 7, Nummer 3, März 2016, S. 1251–1265, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1039/c5fo01530h">10.1039/c5fo01530h</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/26797090?dopt=Abstract">PMID 26797090</a>.</span>
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<li id="cite_note-4"><span class="mw-cite-backlink"><a href="#cite_ref-4">↑</a></span> <span class="reference-text">T. Terada, K. Inui: <i>Recent advances in structural biology of peptide transporters.</i> In: <i>Current topics in membranes.</i> Band 70, 2012, S. 257–274, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1016/B978-0-12-394316-3.00008-9">10.1016/B978-0-12-394316-3.00008-9</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23177989?dopt=Abstract">PMID 23177989</a>.</span>
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<li id="cite_note-5"><span class="mw-cite-backlink"><a href="#cite_ref-5">↑</a></span> <span class="reference-text">A. I. Faden, S. M. Knoblach, V. A. Movsesyan, P. M. Lea, I. Cernak: <i>Novel neuroprotective tripeptides and dipeptides.</i> In: <i>Annals of the New York Academy of Sciences.</i> Band 1053, August 2005, S. 472–481, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1196/annals.1344.041">10.1196/annals.1344.041</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16179555?dopt=Abstract">PMID 16179555</a>.</span>
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<li id="cite_note-6"><span class="mw-cite-backlink"><a href="#cite_ref-6">↑</a></span> <span class="reference-text"><span class="cite"><a rel="nofollow" class="external text" href="https://api.swissmilk.ch/wp-content/uploads/2019/05/studie-bioaktive-peptide-in-milch-und-milchprodukten-ernaehrungswissenschaft.de_.pdf"><i>Studie bioaktive Peptide in Milch und Milchprodukten Enährungswissenschaft.</i></a> (PDF)<span class="Abrufdatum"> Abgerufen am 16. Juli 2022</span>.</span><span style="display: none;" class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2Fde.wikipedia.org%3ATripeptide&rft.title=Studie+bioaktive+Peptide+in+Milch+und+Milchprodukten+En%C3%A4hrungswissenschaft&rft.description=Studie+bioaktive+Peptide+in+Milch+und+Milchprodukten+En%C3%A4hrungswissenschaft&rft.identifier=https%3A%2F%2Fapi.swissmilk.ch%2Fwp-content%2Fuploads%2F2019%2F05%2Fstudie-bioaktive-peptide-in-milch-und-milchprodukten-ernaehrungswissenschaft.de_.pdf"> </span></span>
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<li id="cite_note-7"><span class="mw-cite-backlink"><a href="#cite_ref-7">↑</a></span> <span class="reference-text">Nussberger: <cite style="font-style:italic">Blutdrucksenkende Tripeptide aus der Milch</cite>. In: <cite style="font-style:italic">Therapeutische Umschau</cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>64</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>3</span>, 1. März 2007, <a href="Internationale_Standardnummer_f%C3%BCr_fortlaufende_Sammelwerke" title="Internationale Standardnummer für fortlaufende Sammelwerke">ISSN</a> <span style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://zdb-katalog.de/list.xhtml?t=iss%3D%220040-5930%22&key=cql">0040-5930</a></span>, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>177–179</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1024/0040-5930.64.3.177">10.1024/0040-5930.64.3.177</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Tripeptide&rft.atitle=Blutdrucksenkende+Tripeptide+aus+der+Milch&rft.au=Nussberger&rft.date=2007-03-01&rft.doi=10.1024%2F0040-5930.64.3.177&rft.genre=journal&rft.issn=0040-5930&rft.issue=3&rft.jtitle=Therapeutische+Umschau&rft.pages=177-179&rft.volume=64" style="display:none"> </span></span>
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<li id="cite_note-8"><span class="mw-cite-backlink"><a href="#cite_ref-8">↑</a></span> <span class="reference-text">Keith Bernard Woodford: <cite style="font-style:italic">Casomorphins and Gliadorphins Have Diverse Systemic Effects Spanning Gut, Brain and Internal Organs</cite>. In: <cite style="font-style:italic">International Journal of Environmental Research and Public Health</cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>18</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>15</span>, Januar 2021, <a href="Internationale_Standardnummer_f%C3%BCr_fortlaufende_Sammelwerke" title="Internationale Standardnummer für fortlaufende Sammelwerke">ISSN</a> <span style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://zdb-katalog.de/list.xhtml?t=iss%3D%221660-4601%22&key=cql">1660-4601</a></span>, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>7911</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.3390/ijerph18157911">10.3390/ijerph18157911</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/34360205?dopt=Abstract">PMID 34360205</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8345738/">PMC 8345738</a> (freier Volltext).<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Tripeptide&rft.atitle=Casomorphins+and+Gliadorphins+Have+Diverse+Systemic+Effects+Spanning+Gut%2C+Brain+and+Internal+Organs&rft.au=Keith+Bernard+Woodford&rft.date=2021-01&rft.doi=10.3390%2Fijerph18157911&rft.genre=journal&rft.issn=1660-4601&rft.issue=15&rft.jtitle=International+Journal+of+Environmental+Research+and+Public+Health&rft.pages=7911&rft.pmc=8345738&rft.pmid=34360205&rft.volume=18" style="display:none"> </span></span>
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