کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10154512 | 1666302 | 2019 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Aggregation of the diabetes-related peptide ProIAPP1-48 measured by dynamic light scattering
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Islet amyloid polypeptide (IAPP1-37) or amylin is implicated in the aetiology of diabetes. It is found as amyloid along with its precursor ProIAPP1-48 in the islets of Langerhans in the pancreas. Metals have been implicated in amyloidogenesis of both IAPP and ProIAPP. Herein we have used dynamic light scattering (DLS) to investigate how Al(III) and Cu(II) influence aggregation of ProIAPP1-48 under near-physiological conditions and in a biologically-relevant timeframe. ProIAPP1-48 formed primarily sub-micron particles within 5âmin (e.g. 470ânm at 15μM peptide) that grew to micron-sized particles (1310ânm) within a 30âmin timeframe. Equimolar Al(III) had little influence upon particle size at either 5 (656ânm) or 30âmin (1250ânm) while Cu(II) tended to increase particle size over the same time period (731-1300ânm). It is suggested that any effects of Al(III) and Cu(II) reflected their well known tendencies to support β-sheet or amorphous aggregates of ProIAPP1-48 respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Trace Elements in Medicine and Biology - Volume 51, January 2019, Pages 1-8
Journal: Journal of Trace Elements in Medicine and Biology - Volume 51, January 2019, Pages 1-8
نویسندگان
Emma Shardlow, Cassandra Rao, Roman Sattarov, Ling Wu, Paul E. Fraser, Christopher Exley,