کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8288788 | 1536266 | 2018 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Acceleration of amyloid fibril formation by carboxyl-terminal truncation of human serum amyloid A
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کلمات کلیدی
ATR-FTIRSAAAA amyloidosis - آمیلوئیدوز AAAttenuated Total Reflection-Fourier Transform Infrared - انعکاس مجموع بازتاب-فوریه تبدیل مادون قرمزTem - این استThT - بلهThioflavin T - تیوفلاوین Tcircular dichroism - رنگ تابی دورانیserum amyloid A - سرم آمیلوئید AAmyloid fibril - فیبریل آمیلوئیدTransmission electron microscopy - میکروسکوپ الکترونی عبوریHeparan sulfate - هپاران سولفاتNative chemical ligation - پیوند شیمیایی بومی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Human serum amyloid A (SAA) is a precursor protein of AA amyloidosis. Although the full-length SAA is 104 amino acids long, the C-terminal-truncated SAA lacking mainly residues 77-104 is predominantly deposited in AA amyloidosis. Nevertheless, the amyloid fibril formation of such truncated forms of human SAA has never been investigated. In the present study, we examined the effect of C-terminal truncation on amyloid fibril formation of human SAA induced by heparan sulfate (HS). Circular dichroism (CD) measurements demonstrated that the C-terminal truncation induces a reduced α-helical structure of the SAA molecule. HS-induced increases in thioflavin T fluorescence for SAA (1-76) peptide and less significant increases for full-length SAA were observed. CD spectral changes of SAA (1-76) peptide but not full-length SAA were observed when incubated with HS, although the spectrum was not typical for a β-structure. Fourier transform infrared experiments clearly revealed that SAA (1-76) peptide forms a β-sheet structure. Transmission electron microscopy revealed that short fibrillar aggregates of SAA (1-76) peptides, which became longer with increasing peptide concentrations, were observed under conditions in which full-length SAA scarcely formed fibrillar aggregates. These results suggested that the C-terminal truncation of human SAA accelerates amyloid fibril formation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 639, 1 February 2018, Pages 9-15
Journal: Archives of Biochemistry and Biophysics - Volume 639, 1 February 2018, Pages 9-15
نویسندگان
Masafumi Tanaka, Toru Kawakami, Nozomi Okino, Kaoru Sasaki, Kiwako Nakanishi, Hiroka Takase, Toshiyuki Yamada, Takahiro Mukai,