Experimental evidence for the reorganization of β-strands within aggregates of the Aβ(16-22) peptide

Journal of the American Chemical Society

Volumn 127, Issue 39, 2005, Pages 13488-13489

  Petty, Sarah A ^a   Decatur, Sean M ^a  

^a MOUNT HOLYOKE COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-28]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[10-23]; AMYLOID BETA PROTEIN[10-35]; AMYLOID BETA PROTEIN[16-22]; AMYLOID BETA PROTEIN[26-33]; AMYLOID BETA PROTEIN[34-42]; AMYLOID BETA PROTEIN[9-25]; CARBON 13; CARBONYL DERIVATIVE; MONOMER; PRION PROTEIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BIOACCUMULATION; CHEMICAL BOND; HUMAN; INFRARED SPECTROSCOPY; NEUROTOXICITY; NON INSULIN DEPENDENT DIABETES MELLITUS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; KINETICS; PEPTIDE FRAGMENTS;

EID: 25844493690     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja054663y     Document Type: Article

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21. 2) were synthesized on a Pioneer peptide synthesizer using standard Fmoc chemical techniques. The peptides were cleaved from the resin using a trifluoroacetic acid/ triisopropylsilane/water mixture, purified by reverse-phase HPLC, characterized by electrospray mass spectrometry. and exchanged in 0.05 mM DC1 for 6-8 h.
22. -1 and averaging over 512 scans. Spectra were collected at 25-75 °C in 10° intervals. The sample temperature was maintained at 75 °C for 3 h before re-equilibrating at 25 °C and recording a final IR spectrum.
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