[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"dispatch-exceptions":3,"glossary-dpp-4":6},{"skip":4,"extra":5},[],[],{"id":7,"slug":8,"term":9,"definition":10,"related_product_ids":11,"related_resource_ids":12,"meta_description":13,"term_i18n":14,"definition_i18n":17,"status":21,"created_at":22,"updated_at":23,"meta_description_i18n":24,"brand":28,"relatedProducts":29,"relatedResources":30,"relatedArticles":31},"4daa14ce-28b8-4373-a3e6-93547bb7e6e6","dpp-4","DPP-4 (Dipeptidyl-Peptidase 4)","La \u003Cstrong>DPP-4\u003C/strong> (\u003Cem>Dipeptidyl-Peptidase 4\u003C/em>, également appelée \u003Cem>CD26\u003C/em> ou \u003Cem>ADA-binding protein\u003C/em>, EC 3.4.14.5) est une \u003Cem>sérine protéase transmembranaire\u003C/em> de type II ubiquitairement exprimée (épithéliums intestinaux, rénaux, endothélium vasculaire, lymphocytes T, hépatocytes), avec une forme soluble circulante libérée par clivage par ADAM17/metalloproteases. Elle clive spécifiquement le dipeptide N-terminal \u003Cstrong>Xaa-Pro\u003C/strong> ou \u003Cstrong>Xaa-Ala\u003C/strong> (avec Pro ou Ala en position 2) des peptides et protéines, exposant un nouveau N-terminal généralement inactivé biologiquement.\n\n\u003Cstrong>Substrats physiologiques\u003C/strong>. La DPP-4 est responsable de l'inactivation rapide de nombreux peptides bioactifs : \u003Cem>GLP-1\u003C/em> (7-37 → 9-37, demi-vie <2 min), \u003Cem>GIP\u003C/em> (1-42 → 3-42, demi-vie ~7 min), \u003Cem>GHRH\u003C/em> (1-44 → 3-44, demi-vie ~7 min), \u003Cem>GRP\u003C/em>, \u003Cem>substance P\u003C/em>, \u003Cem>neuropeptide Y\u003C/em> (NPY 1-36 → 3-36, switch Y1→Y2/Y5), \u003Cem>BNP/ANP\u003C/em>, \u003Cem>PYY\u003C/em> (1-36 → 3-36, conversion PYY3-36 plus actif), \u003Cem>chimiokines\u003C/em> (CXCL10, CCL5/RANTES, IP-10) et facteurs hématopoïétiques (SDF-1α/CXCL12, G-CSF). Cette activité régule à la fois la sécrétion d'insuline, la chimiotaxie lymphocytaire et l'axe GH.\n\n\u003Cstrong>Inhibiteurs thérapeutiques\u003C/strong>. Les \u003Cem>gliptines\u003C/em> (inhibiteurs compétitifs DPP-4) constituent une classe majeure d'antidiabétiques oraux : \u003Cem>sitagliptine\u003C/em> (Januvia®, Merck, 2006), \u003Cem>vildagliptine\u003C/em> (Galvus®, Novartis), \u003Cem>saxagliptine\u003C/em> (Onglyza®, BMS), \u003Cem>linagliptine\u003C/em> (Tradjenta®, Boehringer), \u003Cem>alogliptine\u003C/em> (Nesina®, Takeda). Elles augmentent la demi-vie endogène du GLP-1 et GIP de 2-3x, améliorant HbA1c de 0.5-0.8% avec profil de sécurité favorable (pas de prise de poids, rare hypoglycémie, controverse pancreatite résolue).\n\n\u003Cstrong>Stratégie de résistance en design peptidique\u003C/strong>. Pour contourner l'inactivation DPP-4 des peptides thérapeutiques, trois stratégies sont utilisées : (1) \u003Cem>substitution Pro2→Aib\u003C/em> (exénatide, sémaglutide, tirzepatide), (2) \u003Cem>substitution Ala2→D-Ala ou Gly\u003C/em> (CJC-1295, liraglutide), (3) \u003Cem>acylation lipidique\u003C/em> prolongée + liaison albumine qui stéralise l'accès DPP-4. Ces modifications prolongent la demi-vie plasmatique de minutes à jours et rendent possible l'administration hebdomadaire (sémaglutide, tirzépatide, rétatrutide).",[],[],"DPP-4 : sérine protéase clivant les dipeptides N-terminaux Xaa-Pro/Xaa-Ala. Inactive GLP-1, GIP, GHRH. Cible thérapeutique (gliptines).",{"de":15,"en":9,"es":16},"DPP-4 (Dipeptidylpeptidase 4)","DPP-4 (dipeptidil peptidasa 4)",{"de":18,"en":19,"es":20},"\u003Cstrong>DPP-4\u003C/strong> (\u003Cem>Dipeptidylpeptidase 4\u003C/em>, auch \u003Cem>CD26\u003C/em> oder \u003Cem>ADA-bindendes Protein\u003C/em> genannt, EC 3.4.14.5) ist eine \u003Cem>Typ-II-Transmembran-Serinprotease\u003C/em>, die ubiquitär exprimiert wird (Darm- und Nierenepithel, Gefäßendothel, T-Lymphozyten, Hepatozyten) und eine zirkulierende lösliche Form besitzt, die durch Spaltung über ADAM17/Metalloproteasen freigesetzt wird. Sie spaltet spezifisch das N-terminale Dipeptid \u003Cstrong>Xaa-Pro\u003C/strong> oder \u003Cstrong>Xaa-Ala\u003C/strong> (mit Pro oder Ala an Position 2) von Peptiden und Proteinen ab und legt dabei einen neuen N-Terminus frei, der in der Regel biologisch inaktiviert ist.\n\n\u003Cstrong>Physiologische Substrate\u003C/strong>. DPP-4 ist für die rasche Inaktivierung zahlreicher bioaktiver Peptide verantwortlich: \u003Cem>GLP-1\u003C/em> (7-37 → 9-37, Halbwertszeit <2 min), \u003Cem>GIP\u003C/em> (1-42 → 3-42, Halbwertszeit ~7 min), \u003Cem>GHRH\u003C/em> (1-44 → 3-44, Halbwertszeit ~7 min), \u003Cem>GRP\u003C/em>, \u003Cem>Substanz P\u003C/em>, \u003Cem>Neuropeptid Y\u003C/em> (NPY 1-36 → 3-36, Wechsel Y1→Y2/Y5), \u003Cem>BNP/ANP\u003C/em>, \u003Cem>PYY\u003C/em> (1-36 → 3-36, Umwandlung in das aktivere PYY3-36), \u003Cem>Chemokine\u003C/em> (CXCL10, CCL5/RANTES, IP-10) sowie hämatopoetische Faktoren (SDF-1α/CXCL12, G-CSF). Diese Aktivität reguliert die Insulinsekretion, die Lymphozyten-Chemotaxis und die GH-Achse.\n\n\u003Cstrong>Therapeutische Hemmstoffe\u003C/strong>. Die \u003Cem>Gliptine\u003C/em> (kompetitive DPP-4-Hemmer) bilden eine wichtige Klasse oraler Antidiabetika: \u003Cem>Sitagliptin\u003C/em> (Januvia®, Merck, 2006), \u003Cem>Vildagliptin\u003C/em> (Galvus®, Novartis), \u003Cem>Saxagliptin\u003C/em> (Onglyza®, BMS), \u003Cem>Linagliptin\u003C/em> (Tradjenta®, Boehringer), \u003Cem>Alogliptin\u003C/em> (Nesina®, Takeda). Sie verlängern die Halbwertszeit von endogenem GLP-1 und GIP um das 2-3x und senken den HbA1c um 0.5-0.8% bei günstigem Sicherheitsprofil (keine Gewichtszunahme, seltene Hypoglykämien, ausgeräumte Pankreatitis-Kontroverse).\n\n\u003Cstrong>Resistenzstrategie im Peptiddesign\u003C/strong>. Um die Inaktivierung therapeutischer Peptide durch DPP-4 zu umgehen, werden drei Strategien eingesetzt: (1) \u003Cem>Substitution Pro2→Aib\u003C/em> (Exenatid, Semaglutid, Tirzepatid), (2) \u003Cem>Substitution Ala2→D-Ala oder Gly\u003C/em> (CJC-1295, Liraglutid), (3) verlängerte \u003Cem>Lipidacylierung\u003C/em> + Albuminbindung, die den Zugang von DPP-4 sterisch blockiert. Diese Modifikationen verlängern die Plasmahalbwertszeit von Minuten auf Tage und ermöglichen eine wöchentliche Verabreichung (Semaglutid, Tirzepatid, Retatrutid).","\u003Cstrong>DPP-4\u003C/strong> (\u003Cem>Dipeptidyl-Peptidase 4\u003C/em>, also called \u003Cem>CD26\u003C/em> or \u003Cem>ADA-binding protein\u003C/em>, EC 3.4.14.5) is a \u003Cem>type II transmembrane serine protease\u003C/em> ubiquitously expressed (intestinal, renal epithelia, vascular endothelium, T lymphocytes, hepatocytes), with a circulating soluble form released by ADAM17/metalloprotease cleavage. It specifically cleaves the \u003Cstrong>Xaa-Pro\u003C/strong> or \u003Cstrong>Xaa-Ala\u003C/strong> N-terminal dipeptide (with Pro or Ala at position 2) of peptides and proteins, exposing a new N-terminus generally biologically inactivated.\n\n\u003Cstrong>Physiological substrates\u003C/strong>. DPP-4 is responsible for rapid inactivation of many bioactive peptides: \u003Cem>GLP-1\u003C/em> (7-37 → 9-37, half-life <2 min), \u003Cem>GIP\u003C/em> (1-42 → 3-42, half-life ~7 min), \u003Cem>GHRH\u003C/em> (1-44 → 3-44, half-life ~7 min), \u003Cem>GRP\u003C/em>, \u003Cem>substance P\u003C/em>, \u003Cem>neuropeptide Y\u003C/em> (NPY 1-36 → 3-36, Y1→Y2/Y5 switch), \u003Cem>BNP/ANP\u003C/em>, \u003Cem>PYY\u003C/em> (1-36 → 3-36, conversion to more active PYY3-36), \u003Cem>chemokines\u003C/em> (CXCL10, CCL5/RANTES, IP-10) and haematopoietic factors (SDF-1α/CXCL12, G-CSF). This activity regulates insulin secretion, lymphocyte chemotaxis and the GH axis.\n\n\u003Cstrong>Therapeutic inhibitors\u003C/strong>. \u003Cem>Gliptins\u003C/em> (competitive DPP-4 inhibitors) constitute a major class of oral antidiabetics: \u003Cem>sitagliptin\u003C/em> (Januvia®, Merck, 2006), \u003Cem>vildagliptin\u003C/em> (Galvus®, Novartis), \u003Cem>saxagliptin\u003C/em> (Onglyza®, BMS), \u003Cem>linagliptin\u003C/em> (Tradjenta®, Boehringer), \u003Cem>alogliptin\u003C/em> (Nesina®, Takeda). They increase endogenous GLP-1 and GIP half-life by 2-3x, improving HbA1c by 0.5-0.8% with favourable safety profile (no weight gain, rare hypoglycaemia, resolved pancreatitis controversy).\n\n\u003Cstrong>Resistance strategy in peptide design\u003C/strong>. To bypass DPP-4 inactivation of therapeutic peptides, three strategies are used: (1) \u003Cem>Pro2→Aib substitution\u003C/em> (exenatide, semaglutide, tirzepatide), (2) \u003Cem>Ala2→D-Ala or Gly substitution\u003C/em> (CJC-1295, liraglutide), (3) extended \u003Cem>lipid acylation\u003C/em> + albumin binding sterically blocking DPP-4 access. These modifications extend plasma half-life from minutes to days and enable weekly administration (semaglutide, tirzepatide, retatrutide).","\u003Cstrong>La DPP-4\u003C/strong> (\u003Cem>dipeptidil peptidasa 4\u003C/em>, también llamada \u003Cem>CD26\u003C/em> o \u003Cem>proteína de unión a ADA\u003C/em>, EC 3.4.14.5) es una \u003Cem>serina proteasa transmembrana de tipo II\u003C/em> de expresión ubicua (epitelios intestinal y renal, endotelio vascular, linfocitos T, hepatocitos), con una forma soluble circulante liberada por escisión mediante ADAM17/metaloproteasa. Escinde específicamente el dipéptido N-terminal \u003Cstrong>Xaa-Pro\u003C/strong> o \u003Cstrong>Xaa-Ala\u003C/strong> (con Pro o Ala en posición 2) de péptidos y proteínas, y deja expuesto un nuevo extremo N-terminal, generalmente inactivado desde el punto de vista biológico.\n\n\u003Cstrong>Sustratos fisiológicos\u003C/strong>. La DPP-4 es responsable de la rápida inactivación de numerosos péptidos bioactivos: \u003Cem>GLP-1\u003C/em> (7-37 → 9-37, semivida <2 min), \u003Cem>GIP\u003C/em> (1-42 → 3-42, semivida ~7 min), \u003Cem>GHRH\u003C/em> (1-44 → 3-44, semivida ~7 min), \u003Cem>GRP\u003C/em>, \u003Cem>sustancia P\u003C/em>, \u003Cem>neuropéptido Y\u003C/em> (NPY 1-36 → 3-36, cambio Y1→Y2/Y5), \u003Cem>BNP/ANP\u003C/em>, \u003Cem>PYY\u003C/em> (1-36 → 3-36, conversión en PYY3-36, más activo), \u003Cem>quimiocinas\u003C/em> (CXCL10, CCL5/RANTES, IP-10) y factores hematopoyéticos (SDF-1α/CXCL12, G-CSF). Esta actividad regula la secreción de insulina, la quimiotaxis linfocitaria y el eje de la GH.\n\n\u003Cstrong>Inhibidores terapéuticos\u003C/strong>. Las \u003Cem>gliptinas\u003C/em> (inhibidores competitivos de la DPP-4) constituyen una clase importante de antidiabéticos orales: \u003Cem>sitagliptina\u003C/em> (Januvia®, Merck, 2006), \u003Cem>vildagliptina\u003C/em> (Galvus®, Novartis), \u003Cem>saxagliptina\u003C/em> (Onglyza®, BMS), \u003Cem>linagliptina\u003C/em> (Tradjenta®, Boehringer), \u003Cem>alogliptina\u003C/em> (Nesina®, Takeda). Multiplican por 2-3x la semivida del GLP-1 y del GIP endógenos y mejoran la HbA1c en un 0.5-0.8%, con un perfil de seguridad favorable (sin aumento de peso, hipoglucemias raras, controversia sobre la pancreatitis resuelta).\n\n\u003Cstrong>Estrategia de resistencia en el diseño de péptidos\u003C/strong>. Para eludir la inactivación de los péptidos terapéuticos por la DPP-4 se emplean tres estrategias: (1) \u003Cem>sustitución Pro2→Aib\u003C/em> (exenatida, semaglutida, tirzepatida), (2) \u003Cem>sustitución Ala2→D-Ala o Gly\u003C/em> (CJC-1295, liraglutida), (3) \u003Cem>acilación lipídica\u003C/em> extendida + unión a la albúmina, que bloquea estéricamente el acceso de la DPP-4. Estas modificaciones prolongan la semivida plasmática de minutos a días y permiten la administración semanal (semaglutida, tirzepatida, retatrutida).","published","2026-04-23T16:14:10.756402+00:00","2026-09-25T10:28:07.921094+00:00",{"de":25,"en":26,"es":27},"DPP-4: Serinprotease, spaltet N-terminale Xaa-Pro/Xaa-Ala-Dipeptide. Inaktiviert GLP-1, GIP, GHRH. Therapeutisches Ziel (Gliptine).","DPP-4: serine protease cleaving N-terminal Xaa-Pro/Xaa-Ala dipeptides. Inactivates GLP-1, GIP, GHRH. Therapeutic target (gliptins).","DPP-4: serina proteasa que escinde los dipéptidos N-terminales Xaa-Pro/Xaa-Ala. Inactiva GLP-1, GIP, GHRH. Diana terapéutica (gliptinas).","lab",[],[],[32,50,60],{"id":33,"slug":34,"title":35,"excerpt":36,"image":37,"published_at":38,"topic":39},"ff0eb393-ba33-4489-9fba-25817137bb27","analytique-peptidique-lcms-rmn-hplc-edman-guide-complet-recherche","Analytique peptidique : LC-MS haute résolution, RMN, HPLC et Edman - Guide complet recherche","Décryptez la caractérisation complète d'un peptide : RP-HPLC préparative et analytique, LC-MS haute résolution Orbitrap/QTOF, RMN 2D (COSY/TOCSY/NOESY), dégradation d'Edman, cartographie peptidique MS/MS, dichroïsme circulaire. Les 10 techniques qui séparent un peptide research-grade d'un peptide douteux, avec seuils de détection et stratégie de QC.","https://dwomsbawthlktapmtmqu.supabase.co/storage/v1/object/public/news-images/news/analytique-peptidique-lcms-rmn-hplc-edman-guide-complet-recherche/couverture-v1.webp","2026-04-24T10:19:48.59696+00:00",{"id":40,"slug":41,"brand":28,"image":42,"label":43,"created_at":44,"label_i18n":45,"description":47,"description_i18n":48},"76bb3e2d-d0c7-41aa-a59c-32f4c77379e9","recherche","https://dwomsbawthlktapmtmqu.supabase.co/storage/v1/object/public/topic-images/topics/rubrique-recherche/vignette-v1.webp","Recherche & Innovation","2025-12-09T19:04:45.271481+00:00",{"en":46},"Research & Innovation","Les dernières avancées sur les peptides.",{"en":49},"The latest advances in peptides.",{"id":51,"slug":52,"title":53,"excerpt":54,"image":55,"published_at":56,"topic":57},"5900cbe0-c896-4d59-a1ea-d9a3869ffa4c","stabilite-peptidique-degradation-lyophilisation-stockage-guide-complet-recherche","Stabilite peptidique : degradation, lyophilisation et stockage - Guide de reference pour la recherche","Maitrisez les mecanismes qui detruisent vos peptides : oxydation Met, deamidation Asn, hydrolyse, aggregation. Protocoles de lyophilisation, conditions de stockage, reconstitution optimale et QC shelf-life. Le pilier technique que tout laboratoire doit integrer pour garantir l'integrite de ses peptides en recherche exploratoire.","https://dwomsbawthlktapmtmqu.supabase.co/storage/v1/object/public/news-images/news/stabilite-peptidique-degradation-lyophilisation-stockage-guide-complet-recherche/couverture-v1.webp","2026-04-23T17:18:00.045625+00:00",{"id":40,"slug":41,"brand":28,"image":42,"label":43,"created_at":44,"label_i18n":58,"description":47,"description_i18n":59},{"en":46},{"en":49},{"id":61,"slug":62,"title":63,"excerpt":64,"image":65,"published_at":66,"topic":67},"7c16228a-35d3-4278-8ce5-5fd119dc2f11","retatrutide-guide-complet-triple-agoniste-ly3437943-recherche","Retatrutide (LY3437943) : guide complet du triple agoniste","Structure, mécanisme triple agoniste, pharmacocinétique, programme TRIUMPH (1-4, Obesity, HFpEF, MASH), comparaison versus semaglutide et tirzepatide, protocoles de reconstitution RUO, stabilité et perspectives réglementaires. Le pilier scientifique de référence sur le retatrutide.","https://dwomsbawthlktapmtmqu.supabase.co/storage/v1/object/public/news-images/news/retatrutide-guide-complet-triple-agoniste-ly3437943-recherche/couverture-v1.webp","2026-04-23T16:33:37.539604+00:00",{"id":40,"slug":41,"brand":28,"image":42,"label":43,"created_at":44,"label_i18n":68,"description":47,"description_i18n":69},{"en":46},{"en":49}]