Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix

2012 ◽  
Vol 422 (4) ◽  
pp. 551-555 ◽  
Author(s):  
Samuel Sparks ◽  
Gai Liu ◽  
Kevin J. Robbins ◽  
Noel D. Lazo
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
The Self ◽  
Islet Amyloid ◽  
Α Helix

scholarly journals Identification of a Specific Residue Side Chain Controlling the Self-Assembly and Cytotoxicity of Islet Amyloid Polypeptide

2018 ◽  
Vol 114 (3) ◽  
pp. 77a-78a
Author(s):  
Phuong Trang Nguyen ◽  
Elizabeth Godin ◽  
Ximena Zottig ◽  
Steve Bourgault
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
The Self ◽  
Side Chain ◽  
Islet Amyloid

New peptide inhibitors modulate the self-assembly of islet amyloid polypeptide residues 11–20 in vitro

2017 ◽  
Vol 804 ◽  
pp. 102-110 ◽  
Author(s):  
Yexuan Mao ◽  
Lanlan Yu ◽  
Ran Yang ◽  
Chuanguo Ma ◽  
Lingbo Qu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
Peptide Inhibitors ◽  
The Self ◽  
Islet Amyloid

Low generation anionic dendrimers modulate islet amyloid polypeptide self-assembly and inhibit pancreatic β-cell toxicity

RSC Advances ◽  
2016 ◽  
Vol 6 (80) ◽  
pp. 76360-76369 ◽  
Author(s):  
Phuong T. Nguyen ◽  
Rishi Sharma ◽  
Rabindra Rej ◽  
Carole Anne De Carufel ◽  
René Roy ◽  
...  
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
The Self ◽  
Pancreatic Β Cell ◽  
Cell Toxicity ◽  
Β Cell ◽  
Islet Amyloid

The self-assembly and cytotoxicity of the amyloidogenic peptide IAPP can be controlled with low generation anionic dendrimers.

Kinetic and Conformational Insights into Islet Amyloid Polypeptide Self-Assembly Using a Biarsenical Fluorogenic Probe

2018 ◽  
Vol 29 (2) ◽  
pp. 517-527 ◽  
Author(s):  
Noé Quittot ◽  
Mathew Sebastiao ◽  
Soultan Al-Halifa ◽  
Steve Bourgault
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Fluorogenic Probe

scholarly journals Synthetic α-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation

2009 ◽  
Vol 49 (4) ◽  
pp. 736-739 ◽  
Author(s):  
Ishu Saraogi ◽  
James A. Hebda ◽  
Jorge Becerril ◽  
Lara A. Estroff ◽  
Andrew D. Miranker ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Helix Mimetics ◽  
Α Helix

Synthetic α-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation

2009 ◽  
Vol 122 (4) ◽  
pp. 748-751 ◽  
Author(s):  
Ishu Saraogi ◽  
James A. Hebda ◽  
Jorge Becerril ◽  
Lara A. Estroff ◽  
Andrew D. Miranker ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Helix Mimetics ◽  
Α Helix

scholarly journals Amphiphilic oligoamide α-helix peptidomimetics inhibit islet amyloid polypeptide aggregation

2015 ◽  
Vol 56 (23) ◽  
pp. 3670-3673 ◽  
Author(s):  
Oleg V. Kulikov ◽  
Sunil Kumar ◽  
Mazin Magzoub ◽  
Peter C. Knipe ◽  
Ishu Saraogi ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Α Helix

scholarly journals Human islet amyloid polypeptide at the air–aqueous interface: a Langmuir monolayer approach

2012 ◽  
Vol 9 (76) ◽  
pp. 3118-3128 ◽  
Author(s):  
Shanghao Li ◽  
Miodrag Micic ◽  
Jhony Orbulescu ◽  
Jeffrey D. Whyte ◽  
Roger M. Leblanc
Keyword(s):  
Self Assembly ◽  
Islet Amyloid Polypeptide ◽  
Langmuir Monolayer ◽  
Human Islet ◽  
Diabetic Patients ◽  
Brewster Angle Microscopy ◽  
Islet Amyloid ◽  
Type 2 Diabetic Patients ◽  
Human Islet Amyloid Polypeptide ◽  
Time Zero

Human islet amyloid polypeptide (hIAPP) is the source of the major component of the amyloid deposits found in the islets of Langerhans of around 95 per cent type 2 diabetic patients. The formation of aggregates and mature fibrils is thought to be responsible for the dysfunction and death of the insulin-producing pancreatic β-cells. Investigation on the conformation, orientation and self-assembly of the hIAPP at time zero could be beneficial for our understanding of its stability and aggregation process. To obtain these insights, the hIAPP at time zero was studied at the air–aqueous interface using the Langmuir monolayer technique. The properties of the hIAPP Langmuir monolayer at the air–aqueous interface on a NaCl subphase with pH 2.0, 5.6 and 9.0 were examined by surface pressure- and potential-area isotherms, UV–Vis absorption, fluorescence spectroscopy and Brewster angle microscopy. The conformational and orientational changes of the hIAPP Langmuir monolayer under different surface pressures were characterized by p-polarized infrared-reflection absorption spectroscopy, and the results did not show any prominent changes of conformation or orientation. The predominant secondary structure of the hIAPP at the air–aqueous interface was α-helix conformation, with a parallel orientation to the interface during compression. These results showed that the hIAPP Langmuir monolayer at the air–aqueous interface was stable, and no aggregate or domain of the hIAPP at the air–aqueous interface was observed during the time of experiments.

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