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- W2559168560 abstract "β-Sheet conformation is promoted in peptides with amphiphilic design, and stable β-turn formation is favored with the unnatural amino acid d-Pro followed by a flexible residue such as Gly. A 19-residue peptide (B3) was synthesized with alternating hydrophobic and hydrophilic residues connected by symmetrical d-Pro-Gly and Gly-d-Pro turns. B3 forms an oligomeric aggregate, rich in β-sheet conformation, that reversibly transforms into an unordered structure on heating, as evidenced by its temperature-dependent IR spectra. When a dansyl moiety was added to the N terminus of B3, the resulting peptide (B3D) can convert into a fibrillar structure after higher temperature incubation, as detected spectroscopically as well as by TEM. The fibrillization process involves an initial unfolding step monitored by the quenching of dansyl emission; in contrast, subsequent enhanced thioflavin T emission is seen on its binding to the fibril. A possible mechanism is proposed: B3D forms a low-temperature oligomer, which is at least partially unfolded by heat and subsequently reassembles more slowly as a fibril." @default.
- W2559168560 created "2016-12-08" @default.
- W2559168560 creator A5003946481 @default.
- W2559168560 creator A5004857117 @default.
- W2559168560 date "2016-12-28" @default.
- W2559168560 modified "2023-09-27" @default.
- W2559168560 title "Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide" @default.
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- W2559168560 doi "https://doi.org/10.1002/cbic.201600436" @default.
- W2559168560 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27897371" @default.
- W2559168560 hasPublicationYear "2016" @default.
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