کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2828873 | 1570449 | 2010 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Density functional theory analysis and spectral studies on amyloid peptide Aβ(28-35) and its mutants A30G and A30I
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کلمات کلیدی
AβFMOCDFT - DFTFluorescence resonance energy transfer - انتقال انرژی رزونانس FluorescenceFRET - انتقال انرژی رزونانسی فورسترThT - بلهAlzheimer’s disease - بیماری آلزایمرConformational analysis - تجزیه و تحلیل سازگارThioflavin T - تیوفلاوین Tcircular dichroism - رنگ تابی دورانیDensity functional theory - نظریه تابعی چگالیwild-type - نوع وحشیamyloid-β peptide - پپتید آمیلیید ب
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Density functional theory analysis and spectral studies on amyloid peptide Aβ(28-35) and its mutants A30G and A30I Density functional theory analysis and spectral studies on amyloid peptide Aβ(28-35) and its mutants A30G and A30I](/preview/png/2828873.png)
چکیده انگلیسی
Folding and self-assembly of amyloid beta (Aβ) peptide are linked to Alzheimer's disease. To understand the initial stage of amyloid-β peptide aggregation, conformational characteristics of monomers of wild-type (WT) Aβ(28-35) and its mutant peptides A30G and A30I were investigated using density functional theory calculations and experimental studies. Monomeric structures and their relative stabilities were obtained on the basis of systematic structural optimization in the gas-phase and in the aqueous medium. Computations were performed by hybrid Hartree-Fock-Density Functional Theory (HF-DFT) at B3LYP/6-31Gâ level. Experimentally, the conformational transitions in the early stages of the octapeptide Aβ(28-35) and its mutants A30G and A30I in solution were characterized by CD, Thioflavin assay and FRET spectroscopy. Examination of the secondary structures revealed that Aβ(28-35) and its mutant monomers exist in random coil conformation in the aqueous medium in agreement with the theoretical predictions, which upon aging is transformed to sheet with different kinetics. This study deals with the structurally important intermediates and it may help to understand the mechanism of amyloid fibril aggregation leading to the onset of Alzheimer's disease.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 170, Issue 3, June 2010, Pages 439-450
Journal: Journal of Structural Biology - Volume 170, Issue 3, June 2010, Pages 439-450
نویسندگان
Sureshbabu Nagarajan, Jayakumar Rajadas, E.J. Padma Malar,