A tale of two tails: Self-assembling properties of A- and B-chain parts of insulin's highly amyloidogenic H-fragment

Due to the spontaneous transition of native insulin into therapeutically inactive amyloid, prolonged storage decreases effectiveness of the hormone in treatment of diabetes. Various regions of the amino acid sequence have been implicated in insulin aggregation. Here, we focus on smaller fragments of...

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Bibliographic Details
Main Authors:	Dec, R. (Author), Dzwolak, W. (Author)
Format:	Article
Language:	English
Published:	Elsevier B.V. 2021
Subjects:	A chain insulin absorption lag time agglomeration amino acid sequence Amino Acid Sequence Amyloid amyloid protein Amyloid stretch amyloidogenecity amyloidogenic activity Amyloidogenic Proteins Article atomic force microscopy attenuated total reflectance Fourier transform infrared spectroscopy B chain insulin band frequency binding affinity binding site chemistry chromophore assisted light inactivation clinical effectiveness Co-aggregation conformational dynamics conformational transition Cross-seeding disulfide bond Disulfide bond fibrillization fluorescence genetic fingerprinting guanidine hydrogen bond Hydrogen-Ion Concentration infrared spectroscopy insulin Insulin insulin aggregation kinetics Kinetics molecular dynamics monomer morphology neutral pH N-termini peptide fragment Peptide fragments Peptide Fragments pH protein aggregate Protein Aggregates protein domain Protein Interaction Domains and Motifs protein multimerization Protein Multimerization protein quaternary structure protein secondary structure Protein Structure, Quaternary purification quantum yield static electricity synthesis thermodynamics tubulin polymerization assay unclassified drug
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A tale of two tails: Self-assembling properties of A- and B-chain parts of insulin's highly amyloidogenic H-fragment

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