Genomics Research Center, Academia Sinica, 128, Academia Road, Section 2, Nankang, Taipei 115, Taiwan; Institute of Biochemistry and Molecular Biology, National Yang-Ming University, 155, Linong Street, Section 2, Taipei 112, Taiwan.
Department of Chemistry, National Taiwan Normal University, 162, Section 1, Heping East Road, Taipei 106, Taiwan.
Eur J Med Chem. 2018 Jan 20;144:626-634. doi: 10.1016/j.ejmech.2017.12.036. Epub 2017 Dec 12.
A series of 3S,4S,5S-trihydroxylated piperidines bearing structural diversity at C-2 or C-6 positions has been synthesized and tested to determine their ability to stabilize the activity of recombinant human α-Galactosidase A (rh-α-Gal A). Hit molecules were identified by rapid inhibitory activity screening, and then further investigated for their ability to protect this enzyme from thermo-induced denaturation and enhance its activity in Fabry patient cell lines. Our study resulted in the identification of a new class of small molecules as enzyme stabilizers for the potential treatment of Fabry disease. Of these, stabilizer 21 was the most effective, showing a 12-fold increase in rh-α-Gal A activity in Fabry disease cell lines.
已合成了一系列在 C-2 或 C-6 位具有结构多样性的 3S、4S、5S-三羟基哌啶,并对其稳定重组人α-半乳糖苷酶 A(rh-α-Gal A)活性的能力进行了测试。通过快速抑制活性筛选鉴定出有效分子,然后进一步研究它们保护该酶免受热诱导变性和提高其在法布里病患者细胞系中活性的能力。我们的研究鉴定出了一类新的小分子作为法布里病潜在治疗药物的酶稳定剂。其中,稳定剂 21 的效果最为显著,使法布里病细胞系中 rh-α-Gal A 的活性提高了 12 倍。