کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1938347 | 1050738 | 2007 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
BTM-P1 polycationic peptide biological activity and 3D-dimensional structure
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The novel BTM-P1 peptide interferes with energetic processes in mitochondria; its antimicrobial activity against Gram-positive and Gram-negative bacteria is described here. BTM-P1 three-dimensional structure was determined by 1H NMR to explain its biological mechanisms and membrane activity. Structural data indicated that BTM-P1 can form an α-helix; circular dichroism analysis confirmed the peptide’s propensity to behave as a typical transmembrane helix in a lipidic environment. According to the structural characteristics of the polycationic BTM-P1 peptide so revealed, its biological activity can be explained by a mechanism involving the formation of ion-permeable channels in biomembranes.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 353, Issue 4, 23 February 2007, Pages 908–914
Journal: Biochemical and Biophysical Research Communications - Volume 353, Issue 4, 23 February 2007, Pages 908–914
نویسندگان
César Segura, Fanny Guzmán, Luz Mary Salazar, Manuel E. Patarroyo, Sergio Orduz, Victor Lemeshko,