Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ1-42 peptide, synthesized by depsi-peptide technique

Biosensors and Bioelectronics

Volumn 26, Issue 5, 2011, Pages 2772-2775

  Stravalaci, Matteo ^a   Beeg, Marten ^a   Salmona, Mario ^a   Gobbi, Marco ^a  

^a MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

Author keywords

Amyloid peptides; Depsi peptides; Fibril elongation; Polymerization kinetics; Surface plasmon resonance

Indexed keywords

AGGREGATION PROPENSITY; ALZHEIMER DISEASE; AMYLOID FIBRIL; AMYLOIDOGENIC PEPTIDES; BINDING AFFINITIES; BINDING PROPERTIES; DEPSI-PEPTIDES; ELONGATION PROCESS; FIBRIL ELONGATION; FIBRIL GROWTH; FREE SOLUTIONS; HUMAN DISEASE; MOLECULAR UNITS; PLASMON RESONANCES; POLYMERIZATION KINETICS; POLYMERIZATION REACTION; PROTEIN AGGREGATES; PUTATIVE LIGANDS; REAL TIME; SEQUENTIAL POLYMERIZATION; SURFACE PLASMONS; SYNTHETIC STRATEGIES; TIME-SCALES;

BINDING ENERGY; ECOLOGY; ELONGATION; GLYCOPROTEINS; GROWTH KINETICS; MONOMERS; ORGANIC POLYMERS; PEPTIDES; PLASMONS; POLYMERIZATION; POLYMERS;

SURFACE PLASMON RESONANCE;

AMYLOID BETA PROTEIN[1-42];

ALZHEIMER DISEASE; ARTICLE; BINDING AFFINITY; DEPOLYMERIZATION; FIBER; KINETICS; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN POLYMERIZATION; PROTEIN SYNTHESIS; RNA TRANSLATION; SURFACE PLASMON RESONANCE;

AMYLOID BETA-PEPTIDES; KINETICS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SURFACE PLASMON RESONANCE;

RUMEX;

EID: 78650626543     PISSN: 09565663     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bios.2010.10.038     Document Type: Article

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