Studies of Amyloid-Like Fibrillogenesis through β-Sheet-Mediated Self-Assembly of Short Synthetic Peptides

被引：5

作者：

Dutt, Anita ^{[1
]}

Spencer, Elinor C. ^{[2
]}

Howard, Judith A. K. ^{[2
]}

Pramanik, Animesh ^{[1
]}

机构：

[1] Univ Calcutta, Dept Chem, Kolkata 700009, W Bengal, India

[2] Univ Durham, Dept Chem, Durham DH1 3LE, England

来源：

CHEMISTRY & BIODIVERSITY | 2010年 / 7卷 / 02期

关键词：

OMEGA-AMINO ACIDS; SOLID-STATE; FIBRIL FORMATION; PARKINSONS-DISEASE; ALPHA-SYNUCLEIN; LEWY BODIES; HELIX; CONFORMATION; PROTEINS; PARALLEL;

D O I：

10.1002/cbdv.200900050

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Three structurally different types of small peptides, namely, i) Boc-Ile-Aib-Ile-OMe (Aib=alpha-aminoisobutyric acid), ii) Boc-Xx-m-aminobenzoic acid (Xx=beta-Ala and gamma-aminobutyric acid), and iii) Boc-Xx-m-nitroaniline, were found to exhibit beta-sheet-mediated fibrillogenesis in the solid state, revealed by FT-IR, single-crystal X-ray diffraction, and FE-SEM studies. Interestingly, the fibrils grown from peptides 2 and 3 were found to bind with the physiological dye Congo red, a characteristic feature of amyloid fibrils.

引用

页码：363 / 375

页数：13

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