scholarly journals Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors

2017 ◽  
Vol 293 (8) ◽  
pp. 2888-2902 ◽  
Author(s):  
Pascal Krotee ◽  
Sarah L. Griner ◽  
Michael R. Sawaya ◽  
Duilio Cascio ◽  
Jose A. Rodriguez ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

scholarly journals Human Islet Amyloid Polypeptide Fibril Binding to Catalase: A Transmission Electron Microscopy and Microplate Study

2010 ◽  
Vol 10 ◽  
pp. 879-893 ◽  
Author(s):  
Nathaniel G. N. Milton ◽  
J. Robin Harris
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Transmission Electron

The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrilsin vitroandin vivo. Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-β (Aβ) and prion protein (PrP) fibrils. Previous studies have shown that catalase binds to Aβ fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. This study presents a transmission electron microscopy (TEM)—based analysis of fibril formation and the binding of human erythrocyte catalase to IAPP fibrils. The results show that human IAPP 1-37, 8-37, and 20-29 peptides form fibrils with diverse and polymorphic structures. All three forms of IAPP bound catalase, and complexes of IAPP 1-37 or 8-37 with catalase were identified by immunoassay. The binding of biotinylated IAPP to catalase was high affinity with a KDof 0.77nM, and could be inhibited by either human or rat IAPP 1-37 and 8-37 forms. Fibrils formed by the PrP 118-135 peptide with a Gly-Ala-Val-Val sequence also bound catalase. These results suggest that catalase recognizes a Gly-Ala-Ile-Leu—like sequence in amyloid fibril-forming peptides. For IAPP 1-37 and 8-37, the catalase binding was primarily directed towards fibrillar rather than ribbon-like structures, suggesting differences in the accessibility of the human IAPP 24-27 Gly-Ala-Ile-Leu region. This suggests that catalase may be able to discriminate between different structural forms of IAPP fibrils. The ability of catalase to bind IAPP, Aβ, and PrP fibrils demonstrates the presence of similar accessible structural motifs that may be targets for antiamyloid therapeutic development.

scholarly journals Time dependence of NMR observables reveals salient differences in the accumulation of early aggregated species between human islet amyloid polypeptide and amyloid-β

2018 ◽  
Vol 20 (14) ◽  
pp. 9561-9573 ◽  
Author(s):  
Anaïs R. F. Hoffmann ◽  
Lucie Caillon ◽  
Lilian Shadai Salazar Vazquez ◽  
Pierre-Alexandre Spath ◽  
Ludovic Carlier ◽  
...  
Keyword(s):  
Time Dependence ◽  
Islet Amyloid Polypeptide ◽  
Proton Nmr ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Proton NMR shows that IAPP fibril formation does not involve the accumulation of early aggregated species, in contrast with Aβ.

scholarly journals Bleomycin modulates amyloid aggregation in β-amyloid and hIAPP

RSC Advances ◽  
2020 ◽  
Vol 10 (43) ◽  
pp. 25929-25946 ◽  
Author(s):  
Anchala Kumari ◽  
Ritika Sharma ◽  
Nidhi Shrivastava ◽  
Pallavi Somvanshi ◽  
Abhinav Grover
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Human Islet ◽  
Amyloid Aggregation ◽  
Islet Amyloid ◽  
Dual Inhibitor ◽  
Human Islet Amyloid Polypeptide ◽  
Β Amyloid ◽  
Β Sheet

Bleomycin acts as a dual inhibitor against both amyloid β and human islet amyloid polypeptide by binding to the β-sheet grooves considered as the amyloids hotspot.

Fibril growth captured by electrical properties of amyloid- β and human islet amyloid polypeptide

2020 ◽  
Vol 101 (6) ◽  
Author(s):  
Prasoon Awasthi ◽  
Anurag Singh ◽  
Suparna Khatun ◽  
Amar Nath Gupta ◽  
Soumen Das
Keyword(s):  
Electrical Properties ◽  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide

2015 ◽  
Vol 17 (35) ◽  
pp. 23245-23256 ◽  
Author(s):  
Mingzhen Zhang ◽  
Rundong Hu ◽  
Hong Chen ◽  
Yung Chang ◽  
Jie Ma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Type 2 Diabetes ◽  
Alzheimer's Disease ◽  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Epidemiological Studies ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Epidemiological studies have shown that the development of Alzheimer's disease (AD) is associated with type 2 diabetes (T2D), but it still remains unclear how AD and T2D are connected.

Human islet amyloid polypeptide accumulates at similar sites in islets of transgenic mice and humans

Diabetes ◽  
1994 ◽  
Vol 43 (5) ◽  
pp. 640-644 ◽  
Author(s):  
E. J. de Koning ◽  
J. W. Hoppener ◽  
J. S. Verbeek ◽  
C. Oosterwijk ◽  
K. L. van Hulst ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

scholarly journals The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death

Biochimie ◽  
2020 ◽  
Vol 170 ◽  
pp. 26-35 ◽  
Author(s):  
Shadai Salazar Vazquez ◽  
Bertrand Blondeau ◽  
Pierre Cattan ◽  
Mathieu Armanet ◽  
Ghislaine Guillemain ◽  
...  
Keyword(s):  
Cell Death ◽  
Islet Amyloid Polypeptide ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

scholarly journals Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers

RSC Advances ◽  
2021 ◽  
Vol 11 (21) ◽  
pp. 12815-12825
Author(s):  
Yajie Wang ◽  
Feihong Meng ◽  
Tong Lu ◽  
Chunyun Wang ◽  
Fei Li
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Membrane Damage ◽  
Islet Amyloid Polypeptide ◽  
Divalent Metal ◽  
Human Islet ◽  
Divalent Metal Ions ◽  
Islet Amyloid ◽  
Induced Membrane ◽  
Human Islet Amyloid Polypeptide

Their is a counteraction between a decrease in the disruptive ability of metal-associated oligomer species and an increase in the quantity of oligomers promoted by the metal binding in the activity of hIAPP induced membrane damage.

scholarly journals Interactions of human islet amyloid polypeptide with lipid structure of different curvatures

2020 ◽  
Vol 10 (6) ◽  
pp. 412-418
Author(s):  
Le Mei ◽  
Wenhui Shen ◽  
Xuwei Wu ◽  
Jie Liu ◽  
Dechang Li ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Islet Amyloid ◽  
Lipid Structure ◽  
Human Islet Amyloid Polypeptide
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