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  5. 4-Substituted 2-amino-3,4-dihydroquinazolines with a 3-hairpin turn side chain as novel inhibitors of BACE-1
 
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4-Substituted 2-amino-3,4-dihydroquinazolines with a 3-hairpin turn side chain as novel inhibitors of BACE-1

Journal
Bioorganic Chemistry
Journal Volume
95
Pages
103135
Date Issued
2020
Author(s)
Jagtap A.D.
Kondekar N.B.
Hung P.-Y.
Hsieh C.-E.
CHIA-RON YANG  
Chen G.S.
Chern J.-W.
DOI
10.1016/j.bioorg.2019.103135
URI
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85077655539&doi=10.1016%2fj.bioorg.2019.103135&partnerID=40&md5=0df0d6b5224fdd3479e8cc9235b7d506
https://scholars.lib.ntu.edu.tw/handle/123456789/565264
Abstract
Herein, we report the identification, design, and synthesis of a series of 4-substituted 2-amino-3,4-dihydroquinazolines with hairpin turn side chains as novel inhibitors of BACE-1. The dihydroquinazoline derivatives were rationally designed by modifying the amide group and relocating the α -hydrophobic substituent on the hairpin turn side chain of lead compound 2 to the C4-position on the 3,4-dihydroquinazoline scaffold to facilitate interactions with the S1, S2 and S1′ subsites of BACE-1. Among these derivatives, two compounds exhibited potent BACE-1 inhibitory activity: 4-methyl-substituted (22a, BACE-1 CFA IC50 = 0.38 μM; BACE-1 WCA IC50 = 0.14 μM) and 4-cyclohexylmethyl-substituted (22b, BACE-1 CFA IC50 = 0.49 μM; BACE-1 WCA IC50 = 0.14 μM) 2-amino-3,4-dihydroquinazoline, each bearing a side chain of N-cyclohexyl-N-((1-methyl-1H-pyrazol-4-yl)methyl amide. The results suggest that the structural modifications maintain the hairpin turn topology similar to that of compound 2 and provide an additional interaction with the S2 subsite. ? 2019
Subjects
2-amino-3; 4-dihydroquinazolines; Alzheimer's disease; BACE-1; Non-peptidic aspartyl protease inhibitors; Structure-activity relationship
SDGs

[SDGs]SDG3

Other Subjects
beta secretase inhibitor; quinazoline derivative; aspartic proteinase; BACE1 protein, human; enzyme inhibitor; quinazoline derivative; secretase; Article; chemical modification; drug design; drug synthesis; IC50; molecular model; priority journal; structure analysis; chemistry; conformation; dose response; human; metabolism; structure activity relation; synthesis; tumor cell line; Amyloid Precursor Protein Secretases; Aspartic Acid Endopeptidases; Cell Line, Tumor; Dose-Response Relationship, Drug; Enzyme Inhibitors; Humans; Models, Molecular; Molecular Conformation; Quinazolines; Structure-Activity Relationship
Type
journal article

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