Probing the Aggregation and Immune Response of Human Islet Amyloid Polypeptides with Ligand-Stabilized Gold Nanoparticles

2019 ◽  
Vol 11 (11) ◽  
pp. 10462-10471 ◽  
Author(s):  
Ibrahim Javed ◽  
Jiacheng He ◽  
Aleksandr Kakinen ◽  
Ava Faridi ◽  
Wen Yang ◽  
...  
Keyword(s):  
Immune Response ◽  
Gold Nanoparticles ◽  
Human Islet ◽  
Islet Amyloid ◽  
Amyloid Polypeptides

Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides’ connection with antimicrobial peptides

2012 ◽  
Vol 393 (7) ◽  
pp. 641-646 ◽  
Author(s):  
Lan Wang ◽  
Qian Liu ◽  
Jin-Chun Chen ◽  
Yi-Xian Cui ◽  
Bing Zhou ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Lipid Membrane ◽  
Human Islet ◽  
Amyloid Peptide ◽  
Islet Amyloid ◽  
Amyloid Peptides ◽  
Amyloid Polypeptides ◽  
New Evidence ◽  
Insight Into

Abstract Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.

scholarly journals Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides

2013 ◽  
Vol 105 (10) ◽  
pp. 2323-2332 ◽  
Author(s):  
Chetan Poojari ◽  
Dequan Xiao ◽  
Victor S. Batista ◽  
Birgit Strodel
Keyword(s):  
Human Islet ◽  
Membrane Permeation ◽  
Islet Amyloid ◽  
Amyloid Polypeptides

Enhanced optical asymmetry in supramolecular chiroplasmonic assemblies with long-range order

Science ◽  
2021 ◽  
Vol 371 (6536) ◽  
pp. 1368-1374 ◽  
Author(s):  
Jun Lu ◽  
Yao Xue ◽  
Kalil Bernardino ◽  
Ning-Ning Zhang ◽  
Weverson R. Gomes ◽  
...  
Keyword(s):  
Long Range ◽  
Gold Nanorods ◽  
Spectral Shift ◽  
Human Islet ◽  
Range Order ◽  
Long Range Order ◽  
Islet Amyloid ◽  
Strong Polarization ◽  
Amyloid Polypeptides ◽  
Strong Scattering

Chiral assemblies of plasmonic nanoparticles are known for strong circular dichroism but not for high optical asymmetry, which is limited by the unfavorable combination of electrical and magnetic field components compounded by strong scattering. Here, we show that these limitations can be overcome by the long-range organization of nanoparticles in a manner similar to the liquid crystals and found in helical assemblies of gold nanorods with human islet amyloid polypeptides. A strong, polarization-dependent spectral shift and the reduced scattering of energy states with antiparallel orientation of dipoles activated in assembled helices increased optical asymmetry g-factors by a factor of more than 4600. The liquid crystal–like color variations and the nanorod-accelerated fibrillation enable drug screening in complex biological media. Improvement of long-range order can also provide structural guidance for the design of materials with high optical asymmetry.

Glycated Insulin Exacerbates the Cytotoxicity of Human Islet Amyloid Polypeptides: a Vicious Cycle in Type 2 Diabetes

2019 ◽  
Vol 14 (3) ◽  
pp. 486-496 ◽  
Author(s):  
Liang Ma ◽  
Chen Yang ◽  
Lianqi Huang ◽  
Yuchen Chen ◽  
Yang Li ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Human Islet ◽  
Vicious Cycle ◽  
Islet Amyloid ◽  
Amyloid Polypeptides

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

scholarly journals Molecular Dynamics Simulations of Human Islet Amyloid Polypeptide (IAPP) Oligomers and their Interactions with Lipid Bilayers

2011 ◽  
Vol 100 (3) ◽  
pp. 200a-201a ◽  
Author(s):  
Jun Zhao ◽  
Xiang Yu ◽  
Chao Zhao ◽  
Qiuming Wang ◽  
Jie Zheng
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Lipid Bilayers ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Dynamics Simulations

Ruthenium complexes as inhibitors of human islet amyloid polypeptide aggregation, an effect that prevents beta cell apoptosis

RSC Advances ◽  
2015 ◽  
Vol 5 (23) ◽  
pp. 17405-17412 ◽  
Author(s):  
Lijuan Ma ◽  
Yuanting Fu ◽  
Lianling Yu ◽  
Xiaoling Li ◽  
Wenjie Zheng ◽  
...  
Keyword(s):  
Beta Cell ◽  
Cell Apoptosis ◽  
Cell Damage ◽  
Islet Amyloid Polypeptide ◽  
Ruthenium Complexes ◽  
Human Islet ◽  
Ros Generation ◽  
Beta Cell Apoptosis ◽  
Islet Amyloid ◽  
Application Potential

Herein we show that ruthenium complexes could inhibit fibrosis of hIAPP and protect the hIAPP-induced cell damage by suppressing ROS generation, indicating the application potential of the complexes in treatment of T2DM by targeting hIAPP.

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