Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity

Biochemistry

Volumn 54, Issue 44, 2015, Pages 6704-6711

  Wang, Hui ^a   Ridgway, Zachary ^a   Cao, Ping ^a,b   Ruzsicska, Bela ^a   Raleigh, Daniel P ^a,c  

^a STONY BROOK UNIVERSITY   (United States)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; MOLECULES; PEPTIDES;

AMYLOID FORMATION; AMYLOIDOGENICITY; GLUCOSE METABOLISM; INSULIN THERAPY; PEPTIDE-BASED INHIBITORS; RECOGNITION ELEMENT; THERAPEUTIC POTENTIALS; TYPE-2 DIABETES;

GLYCOPROTEINS;

AMYLIN; AMYLOID; PRAMLINTIDE; THIOFLAVINE; ANTIDIABETIC AGENT; PROTEIN AGGREGATE;

AMYLOIDOGENICITY; ARTICLE; BETA SHEET; CHEMICAL ANALYSIS; COMPARATIVE STUDY; DIABETES MELLITUS; DRUG MECHANISM; HUMAN; IN VITRO STUDY; INSULIN TREATMENT; MOLECULAR RECOGNITION; NONHUMAN; PANCREAS ISLET; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; RAT; STRUCTURE ANALYSIS; WILD TYPE; AMINO ACID SEQUENCE; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; DRUG EFFECTS; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; HUMANS; HYPOGLYCEMIC AGENTS; ISLET AMYLOID POLYPEPTIDE; MOLECULAR SEQUENCE DATA; PROTEIN AGGREGATES; PROTEIN STRUCTURE, SECONDARY; RATS; SEQUENCE ALIGNMENT;

EID: 84946925999     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00567     Document Type: Article

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