Elongation of the C-terminal domain of an anti-amyloid β single-chain variable fragment increases its thermodynamic stability and decreases its aggregation tendency

mAbs

Volumn 5, Issue 5, 2013, Pages 678-689

  Rivera Hernández, Geovanny ^a   Marin Argany, Marta ^a   Blasco Moreno, Bernat ^a,b   Bonet, Jaume ^b   Oliva, Baldo ^b   Villegas, Sandra ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b UNIVERSITAT POMPEU FABRA   (Spain)

Author keywords

Aggregation; Alzheimer disease; CD; FTIR; Immunotherapy; ScFv; Stability

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; SCFV H3D6; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; UREA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DRUG STABILITY; DRUG STRUCTURE; INFRARED SPECTROSCOPY; THERMOSTABILITY;

AGGREGATION; ALZHEIMER DISEASE; CD; FTIR; IMMUNOTHERAPY; SCFV; STABILITY;

AMYLOID BETA-PEPTIDES; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN LIGHT CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MODELS, MOLECULAR; MUTATION; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; SINGLE-CHAIN ANTIBODIES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; UREA;

EID: 84883876434     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.25382     Document Type: Article

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