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Volumn 120, Issue , 2013, Pages 18-23

Engineered non-fluorescent Affibody molecules facilitate studies of the amyloid-beta (Aβ) peptide in monomeric form: Low pH was found to reduce Aβ/Cu(II) binding affinity

(6) Lindgren, Joel a Segerfeldt, Patrik a Sholts, Sabrina B b,c Gräslund, Astrid c Karlström, Amelie Eriksson a Wärmländer, Sebastian K T S c

a ALBANOVA UNIVERSITY CENTER (Sweden)

b UNIVERSITY OF CALIFORNIA (United States)

c STOCKHOLM UNIVERSITY (Sweden)

Author keywords

Affibody molecule; Alzheimer's disease; Binding constant; Copper ion; Peptide aggregation; Protein engineering

Indexed keywords

AMYLOID BETA PROTEIN; CUPRIC ION; HISTIDINE;

ARTICLE; BINDING AFFINITY; BIOSENSOR; FLUORESCENCE SPECTROSCOPY; METAL BINDING; MOLECULE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTON TRANSPORT; TITRIMETRY;

AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; COPPER; FLUORESCENCE; HISTIDINE; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SURFACE PLASMON RESONANCE;

EID: 84871389016 PISSN: 01620134 EISSN: 18733344 Source Type: Journal
DOI: 10.1016/j.jinorgbio.2012.11.005 Document Type: Article

Times cited : (18)

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