Abstract
The differences in the C-terminal domains of human amylin peptide variants initiate different aggregation processes and differences in the composition of the aggregates by affecting the hydrophobic cores, conformations, and intra-sheet interactions of the peptides, which have distinct effects on the cytotoxicity of the peptides.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antineoplastic Agents / chemistry
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Antineoplastic Agents / pharmacology*
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Cell Line, Tumor
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Cell Survival / drug effects
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Dose-Response Relationship, Drug
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Drug Screening Assays, Antitumor
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Humans
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Hydrophobic and Hydrophilic Interactions
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Islet Amyloid Polypeptide / chemistry
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Islet Amyloid Polypeptide / pharmacology*
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Protein Conformation
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Rats
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Structure-Activity Relationship
Substances
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Antineoplastic Agents
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Islet Amyloid Polypeptide