کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10769991 | 1050827 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Stabilization of the fibrous structure of an α-helix-forming peptide by sequence reversal
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Stabilization of the fibrous structure of an α-helix-forming peptide by sequence reversal Stabilization of the fibrous structure of an α-helix-forming peptide by sequence reversal](/preview/png/10769991.png)
چکیده انگلیسی
The α3-peptide, which comprises three repeats of the sequence Leu-Glu-Thr-Leu-Ala-Lys-Ala and forms an amphipathic α-helix, is unique among various α-helix-forming peptides in that it assembles into fibrous structures that can be observed by transmission electron microscopy. As part of our investigation of the structure-stability relationships of the α3-peptide, we synthesized the r3-peptide, whose amino acid sequence is the reverse of that of the α3-peptide, and we investigated the effects of sequence reversal on α-helix stability and the formation of fibrous structures. Unexpectedly, the r3-peptide formed a more-stable α-helix and longer fibers than did the α3-peptide. The stability of the r3-peptide helix decreased when the ionic strength of the buffer was increased and when the pH of the buffer was adjusted to 2 or 12. These results suggest that the r3-peptide underwent a “magnet-like” oligomerization and that an increase in the charge-distribution inequality may be the driving force for the formation of fibrous structures.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 2, 3 June 2005, Pages 577-582
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 2, 3 June 2005, Pages 577-582
نویسندگان
Shuichi Kojima, Yukino Kuriki, Kazumori Yazaki, Kin-ichiro Miura,