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• W2005787907 endingPage "8958" @default.
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• W2005787907 abstract "Peptides with a combination of hydrophilic and hydrophobic sequences mimicking the primary structure of Bombyx mori silk fibroin were synthesized and studied in the solid state by NMR using 13C selective labeling coupled with 13C conformation-dependent chemical shifts and 2D solid-state spin-diffusion NMR. The hydrophilic sequence was poly(l-glutamic acid) (E)n, and the hydrophobic one was the consensus sequence of the crystalline fraction of B. mori silk fibroin, (AGSGAG)4. The balance of hydrophilic and hydrophobic characters of the peptide was controlled by changing the relative length, n, of (E)n from 4 to 8. When n = 4 and 5, the structure of the hydrophobic sequence is basically Silk I (the structure of B. mori silk fibroin before spinning in the solid state), and the polyglutamate sequences are random coil. On the other hand, when n = 6−8, the structure of the polyglutamate sequence changes gradually from random coil to β-sheet, and the hydrophobic sequence adopts a mixture of β-sheet and random coil/distorted β-turn forms, although the fraction of the latter form decreases gradually by increasing the number n from 6 to 8. Molecular dynamics and molecular mechanics calculations were also performed to examine the stability of the aggregated domains of the peptides in the solid state. The conformational change of (E)4(AGSGAG)4 was monitored in the solid state by decreasing the pH of the aqueous solution during the sample preparation." @default.
• W2005787907 created "2016-06-24" @default.
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• W2005787907 date "2009-10-30" @default.
• W2005787907 modified "2023-10-17" @default.
• W2005787907 title "Structural Characterization of Silk-Based Water-Soluble Peptides (Glu)_<i>n</i>(Ala-Gly-Ser-Gly-Ala-Gly)₄ (<i>n</i> = 4−8) as a Mimic of <i>Bombyx mori</i> Silk Fibroin by ¹³C Solid-State NMR" @default.
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• W2005787907 doi "https://doi.org/10.1021/ma901949x" @default.
• W2005787907 hasPublicationYear "2009" @default.
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