کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8455272 | 1548020 | 2014 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural characterization and biological properties of the amyloidogenic elastin-like peptide (VGGVG)3
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The present study has been undertaken with the aim to characterize a chemically synthesized elastin-like peptide (VGGVG)3. Structural and biological features were compared with those of peptides as poly(VGGVG) and VGGVG that, having the same amino acid sequence, but different length and supramolecular structure have been previously investigated for their amyloidogenic properties. Results demonstrate that a minimum sequence of 15 amino acids is sufficient to aggregate into short amyloid-like fibrils, whose formation is however strictly dependent on the specific VGGVG repeated sequence. Moreover, in the attempt to elucidate the relationship among aggregation properties, fibers morphology and biocompatibility, 3T3 fibroblasts were grown in the presence of VGGVG-containing elastin-like peptides (ELPs) and analyzed for their ability to proliferate, attach and spread on ELPs-coated surfaces. Data clearly show that amyloid-like fibrils made of (VGGVG)3 are not cytotoxic at least up to the concentration of 100 μg/ml, even after several days of culture, and are a good support for cell attachment and spreading.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 36, June 2014, Pages 15-27
Journal: Matrix Biology - Volume 36, June 2014, Pages 15-27
نویسندگان
Pasquale Moscarelli, Federica Boraldi, Brigida Bochicchio, Antonietta Pepe, Anna Maria Salvi, Daniela Quaglino,