Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils

Sedman, Victoria L.; Allen, Stephanie; Chan, Weng C.; Davies, Martyn C.; Roberts, Clive J.; Tendler, Saul J. B.; Williams, Philip M.
January 2005
Protein & Peptide Letters;Jan2005, Vol. 12 Issue 1, p79
Academic Journal
Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our results demonstrate that the amylin(20-29) peptide fragment forms amyloid-like fibrils that display polymorphic structures. Twisting along the axis of fibrils was often observed in fibrils aged for 6 hours but disappeared in mature fibrils aged for longer time periods.


Related Articles

  • Prediction of "hot spots" of aggregation in disease-linked polypeptides. de Groot, Natalia Sánchez; Pallarés, Irantzu; Avilés, Francesc X.; Vendrell, Josep; Salvador Ventura // BMC Structural Biology;2005, Vol. 5, p18 

    Background: The polypeptides involved in amyloidogenesis may be globular proteins with a defined 3D-structure or natively unfolded proteins. The first class includes polypeptides such as β2- microglobulin, lysozyme, transthyretin or the prion protein, whereas β-amyloid peptide, amylin or...

  • On the Folding of Islet Amyloid Polypeptide in Water. Lazo, Noel; Aucoin, Darryl // Diabetes;Jun2007 Supplement 1, Vol. 56, pA683 

    A thirty-seven residue polypeptide named islet amyloid polypeptide (IAPP) is co-secreted by the β cells with insulin. This polypeptide is highly hydrophobic and aggregates to form oligomers that assemble to form fibrils. The formation of oligomers requires monomer folding. We hypothesize that...

  • Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity. Zelus, Casey; Fox, Ayano; Calciano, Anastasia; Faridian, Bianca S.; Nogaj, Luiza A.; Moffet, David A. // Open Biochemistry Journal;2012, Vol. 6, p66 

    The aggregation of the amyloidogenic polypeptide IAPP (Islet Amyloid Polypeptide, amylin) is believed to play a direct role in the death of pancreatic ß-islet cells in type II diabetes. Preventing the initial aggregation event of IAPP is one strategy for slowing, and possibly preventing, the...

  • Amylin receptor: a common pathophysiological target in Alzheimer's Disease and Diabetes Mellitus. Wen Fu; Patel, Aarti; Jhamandas, Jack H. // Frontiers in Aging Neuroscience;Aug2013, Vol. 5, p1 

    Amylin (islet amyloid polypeptide) and amyloid beta protein (Aβ), which are deposited within pancreatic islets of diabetics and brains of Alzheimer's patients respectively, share many biophysical and physiological properties. Emerging evidence indicates that the amylin receptor is a putative...

  • Evaluation of Aluminium, Manganese, Copper and Selenium Effects on Human Islets Amyloid Polypeptide Hormone Aggregation. Mirhashemi, Seyyed Mehdi; Shahabaddin, Mohammad-Esmail // Pakistan Journal of Biological Sciences;2011, Vol. 14 Issue 4, p288 

    No abstract available.

  • Islet amyloid polypeptide promotes beta-cell proliferation in neonatal rat pancreatic islets. Karlsson, E.; Sandler, S. // Diabetologia;Aug2001, Vol. 44 Issue 8, p1015 

    Aims/hypothesis: We aimed to clarify the role of islet amyloid polypeptide, which is expressed at early embryonic onset, in the proliferation and cell death of neonatal islet cells. Methods: Fetal islets were prepared from pregnant rats on gestational day 21. Islets were cultured in RPMI 1640...

  • Pramlintide as a Weight-Loss Adjunct.  // Clinical Oncology Alert;Nov2008 Primary Care Supplement, p22 

    The article discusses research being done on pramlintide as a weight-loss adjunct. It references a study by Smith et al. published in a 2008 issue of "Diabetes Care." The researchers performed a double-blind, placebo-controlled trial of various doses of subcutaneous pramlintide in obese,...

  • Fresh from the pipeline: Exenatide. Davidson, Mayer B.; Bate, Guy; Kirkpatrick, Peter // Nature Reviews Drug Discovery;Sep2005, Vol. 4 Issue 9, p713 

    In April 2005, exenatide (Byetta; Amylin/Eli Lilly) was approved by the US FDA as an adjunctive therapy to improve blood-sugar control in patients with type 2 diabetes. It is the first in a new class of drugs that mimic the activity of natural glucoregulatory peptides known as incretins.

  • Insights into the mechanism of Alzheimer's β-amyloid aggregation as a function of concentration by using atomic force microscopy. Mustata, Gina-Mirela; Shekhawat, Gajendra S.; Lambert, Mary P.; Viola, Kirsten L.; Velasco, Pauline T.; Klein, William L.; Dravid, Vinayak P. // Applied Physics Letters;3/26/2012, Vol. 100 Issue 13, p133704 

    The size and shape of Alzheimer's β-amyloid structures, as well as the kinetics of their self-assembly, exhibits a very pronounced dependence on concentration and environment. In the present study, we are reporting the direct observation of Aβ oligomers and fibrils assemblies using atomic...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics