Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly

Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show...

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Published inNature communications Vol. 13; no. 1; pp. 1040 - 15
Main Authors Xu, Yong, Maya-Martinez, Roberto, Guthertz, Nicolas, Heath, George R., Manfield, Iain W., Breeze, Alexander L., Sobott, Frank, Foster, Richard, Radford, Sheena E.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 24.02.2022
Nature Publishing Group
Nature Portfolio
Subjects
101/6
631/45
631/57
82/58
Agglomeration
Alzheimer's disease
Amylin
Amyloid
Amyloid - metabolism
Amyloidogenesis
Amyloidogenic Proteins - metabolism
Assembly
Binding
Chemical compounds
Chemical kinetics
Diabetes
Diabetes mellitus
Diabetes mellitus (non-insulin dependent)
Diabetes Mellitus, Type 2 - drug therapy
Diabetes Mellitus, Type 2 - metabolism
Drug development
Elongated structure
Elongation
Fibrils
Fluorescence
Humanities and Social Sciences
Humans
Islet Amyloid Polypeptide - metabolism
Islets of Langerhans - metabolism
Kinetics
Lag phase
Mass spectrometry
Mass spectroscopy
Modulators
Molecular biology
Monomers
multidisciplinary
NMR
Nuclear magnetic resonance
Nucleation
Peptides
Polypeptides
Reaction kinetics
Science
Science (multidisciplinary)
Scientific imaging
Titration
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Abstract Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D. Here the authors carry out chemical kinetic studies revealing that aggregation of hIAPP and its variant S20G involves secondary nucleation. Two small molecules with novel scaffolds are shown to inhibit or accelerate aggregation by binding different molecular species.
AbstractList Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D.
Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D.Here the authors carry out chemical kinetic studies revealing that aggregation of hIAPP and its variant S20G involves secondary nucleation. Two small molecules with novel scaffolds are shown to inhibit or accelerate aggregation by binding different molecular species.
Here the authors carry out chemical kinetic studies revealing that aggregation of hIAPP and its variant S20G involves secondary nucleation. Two small molecules with novel scaffolds are shown to inhibit or accelerate aggregation by binding different molecular species.
Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D. Here the authors carry out chemical kinetic studies revealing that aggregation of hIAPP and its variant S20G involves secondary nucleation. Two small molecules with novel scaffolds are shown to inhibit or accelerate aggregation by binding different molecular species.
Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D.Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP and its more amyloidogenic natural variant S20G. We show that the aggregation of both peptides involves primary nucleation, secondary nucleation and elongation. We also report the discovery of two structurally distinct small-molecule modulators of hIAPP assembly, one delaying the aggregation of wt hIAPP, but not S20G; while the other enhances the rate of aggregation of both variants at substoichiometric concentrations. Investigation into the inhibition mechanism(s) using chemical kinetics, native mass spectrometry, fluorescence titration, SPR and NMR revealed that the inhibitor retards primary nucleation, secondary nucleation and elongation, by binding peptide monomers. By contrast, the accelerator predominantly interacts with species formed in the lag phase. These compounds represent useful chemical tools to study hIAPP aggregation and may serve as promising starting-points for the development of therapeutics for T2D.
ArticleNumber 1040
Author Breeze, Alexander L.
Xu, Yong
Guthertz, Nicolas
Manfield, Iain W.
Foster, Richard
Sobott, Frank
Radford, Sheena E.
Maya-Martinez, Roberto
Heath, George R.
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/35210421$$D View this record in MEDLINE/PubMed
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Snippet Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we...
Here the authors carry out chemical kinetic studies revealing that aggregation of hIAPP and its variant S20G involves secondary nucleation. Two small molecules...
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Aggregation Database
Index Database
Publisher
StartPage 1040
SubjectTerms 101/6
631/45
631/57
82/58
Agglomeration
Alzheimer's disease
Amylin
Amyloid
Amyloid - metabolism
Amyloidogenesis
Amyloidogenic Proteins - metabolism
Assembly
Binding
Chemical compounds
Chemical kinetics
Diabetes
Diabetes mellitus
Diabetes mellitus (non-insulin dependent)
Diabetes Mellitus, Type 2 - drug therapy
Diabetes Mellitus, Type 2 - metabolism
Drug development
Elongated structure
Elongation
Fibrils
Fluorescence
Humanities and Social Sciences
Humans
Islet Amyloid Polypeptide - metabolism
Islets of Langerhans - metabolism
Kinetics
Lag phase
Mass spectrometry
Mass spectroscopy
Modulators
Molecular biology
Monomers
multidisciplinary
NMR
Nuclear magnetic resonance
Nucleation
Peptides
Polypeptides
Reaction kinetics
Science
Science (multidisciplinary)
Scientific imaging
Titration
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Title Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly
URI https://link.springer.com/article/10.1038/s41467-022-28660-7
https://www.ncbi.nlm.nih.gov/pubmed/35210421
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