Studies of the β-sheet mediated self-assembly of designed synthetic peptides of general formula PhCO-Gly-Xx-OCH2Ph and the possible role of aromatic π-π interactions in the self-assembly

被引:3
|
作者
Dutta, Arpita [1 ]
Kar, Sudeshna [1 ]
Froehlich, Roland [2 ]
Koley, Pradyot [1 ]
Pramanik, Animesh [1 ]
机构
[1] Univ Calcutta, Dept Chem, Kolkata 700009, W Bengal, India
[2] Univ Munster, Inst Organ Chem, D-48149 Munster, Germany
关键词
Peptides; self-assembly; supramolecular beta-sheet; aromatic pi-pi interactions; ribbon like structures; PARKINSONS-DISEASE; ALPHA-SYNUCLEIN; LEWY BODIES; SOLID-STATE; AMINO-ACIDS; FIBRILS; AGGREGATION; FIBRILLOGENESIS; MINERALIZATION; CONFORMATION;
D O I
10.3998/ark.5550190.0010.724
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
A set of three peptides 1-3 of general formula PhCO-Gly-Xx-OCH2Ph, where Xx is Gly in peptide 1, Ala in 2 and Aib (alpha-animo isobutyric acid) in 3 has been chosen to study the self-assembly and the morphology of the solid biomaterials. FT-IR and single crystal X-ray diffraction studies reveal that the peptides 1-3 self-assemble to form supramolecular beta-sheet structures through intermolecular hydrogen bonds and aromatic pi-pi interactions. Field emission scanning electron micrographs (FE-SEM) of the dried materials of the peptides 1-3 show the formation of flat ribbon like structures which are formed through beta-sheet mediated self-assembly.
引用
收藏
页码:247 / 259
页数:13
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