| 词条 | DAPT (chemical) |
| 释义 |
| ImageFile = DAPT.svg | ImageSize = 200px | IUPACName = tert-Butyl (2S)-2-[[(2S)-2-[[2-(3,5-difluorophenyl)acetyl]amino]propanoyl]amino]-2-phenylacetate | OtherNames = gamma-Secretase Inhibitor IX; GSI-IX; LY-374973; N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester | Section1 = {{Chembox Identifiers | CASNo = 208255-80-5 | PubChem = 5311272 | ChEBI = 86193 | ChemSpiderID = 4470783 | ChEMBL = 255682 | StdInChI=1S/C23H26F2N2O4/c1-14(26-19(28)12-15-10-17(24)13-18(25)11-15)21(29)27-20(16-8-6-5-7-9-16)22(30)31-23(2,3)4/h5-11,13-14,20H,12H2,1-4H3,(H,26,28)(H,27,29)/t14-,20-/m0/s1 | StdInChIKey = DWJXYEABWRJFSP-XOBRGWDASA-N | SMILES = C[C@@H](C(=O)N[C@@H](C1=CC=CC=C1)C(=O)OC(C)(C)C)NC(=O)CC2=CC(=CC(=C2)F)F | Section2 = {{Chembox Properties | C=23|H=26|F=2|N=2|O=4 | Appearance = | Density = | MeltingPt = | BoilingPt = | Solubility = | Section3 = {{Chembox Hazards | MainHazards = | FlashPt = | AutoignitionPt = }}DAPT is a chemical compound used in the study of the Notch signaling pathway.[1] DAPT is a γ-secretase inhibitor. It indirectly inhibits Notch, which is a substrate for γ-secretase.[2] In a mouse model of Alzheimer's disease, DAPT reduces the levels of beta-amyloid.[3] References1. ^{{Cite journal | doi = 10.1093/embo-reports/kvf124 | pmid = 12101103 | pmc = 1084181 | title = A gamma-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish | journal = EMBO Reports | volume = 3 | issue = 7 | pages = 688–694 | year = 2002 | last1 = Geling | first1 = A. | last2 = Steiner | first2 = H. | last3 = Willem | first3 = M. | last4 = Bally-Cuif | first4 = L. | last5 = Haass | first5 = C. }} 2. ^{{Cite web | url = https://www.sigmaaldrich.com/catalog/product/sigma/d5942 | title = DAPT | publisher = Sigma-Aldrich }} 3. ^{{Cite journal | pmid = 11145990| year = 2001| last1 = Dovey| first1 = H. F.| title = Functional gamma-secretase inhibitors reduce beta-amyloid peptide levels in brain| journal = Journal of Neurochemistry| volume = 76| issue = 1| pages = 173–81| last2 = John| first2 = V.| last3 = Anderson| first3 = J. P.| last4 = Chen| first4 = L. Z.| last5 = De Saint Andrieu| first5 = P.| last6 = Fang| first6 = L. Y.| last7 = Freedman| first7 = S. B.| last8 = Folmer| first8 = B.| last9 = Goldbach| first9 = E.| last10 = Holsztynska| first10 = E. J.| last11 = Hu| first11 = K. L.| last12 = Johnson-Wood| first12 = K. L.| last13 = Kennedy| first13 = S. L.| last14 = Kholodenko| first14 = D.| last15 = Knops| first15 = J. E.| last16 = Latimer| first16 = L. H.| last17 = Lee| first17 = M.| last18 = Liao| first18 = Z.| last19 = Lieberburg| first19 = I. M.| last20 = Motter| first20 = R. N.| last21 = Mutter| first21 = L. C.| last22 = Nietz| first22 = J.| last23 = Quinn| first23 = K. P.| last24 = Sacchi| first24 = K. L.| last25 = Seubert| first25 = P. A.| last26 = Shopp| first26 = G. M.| last27 = Thorsett| first27 = E. D.| last28 = Tung| first28 = J. S.| last29 = Wu| first29 = J.| last30 = Yang| first30 = S.| displayauthors = 29| doi = 10.1046/j.1471-4159.2001.00012.x}} 3 : Enzyme inhibitors|Fluoroarenes|Dipeptides |
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