Dutt Anita, Drew Michael G B, Pramanik Animesh
Department of Chemistry, University of Calcutta, 92, A. P. C. Road, Kolkata 700009, India.
Org Biomol Chem. 2005 Jun 21;3(12):2250-4. doi: 10.1039/b504112k. Epub 2005 May 17.
Single crystal X-ray diffraction studies show that the extended structure of dipeptide Boc-beta-Ala-m-ABA-OMe (m-ABA: meta-aminobenzoic acid) self-assembles in the solid state by intermolecular hydrogen bonding to create an infinite parallel beta-sheet structure. In dipeptide Boc-gamma-Abu-m-ABA-OMe (gamma-Abu: gamma-aminobutyric acid), two such parallel beta-sheets are further cross-linked by intermolecular hydrogen bonding through m-aminobenzoic acid moieties. SEM (scanning electron microscopy) studies reveal that both the peptides and form amyloid-like fibrils in the solid state. The fibrils are also found to be stained readily by Congo red, a characteristic feature of the amyloid fiber whose accumulation causes several fatal diseases such as Alzheimer's, prion-protein etc.
单晶X射线衍射研究表明，二肽Boc-β-丙氨酸-间氨基苯甲酸甲酯（m-ABA：间氨基苯甲酸）的扩展结构在固态中通过分子间氢键自组装，形成无限平行的β-折叠结构。在二肽Boc-γ-氨基丁酸-间氨基苯甲酸甲酯（γ-Abu：γ-氨基丁酸）中，两个这样的平行β-折叠通过间氨基苯甲酸部分通过分子间氢键进一步交联。扫描电子显微镜（SEM）研究表明，这两种肽在固态下均形成淀粉样纤维。还发现这些纤维很容易被刚果红染色，这是淀粉样纤维的一个特征，其积累会导致几种致命疾病，如阿尔茨海默病、朊病毒蛋白病等。
