Islet amyloid polypeptide and high hydrostatic pressure: towards an understanding of the fibrillization process

Lopes, Dahabada H. J.; Smirnovas, Vytautas; Winter, Roland

doi:10.1088/1742-6596/121/11/112002

Cited by 2 publications

(2 citation statements)

References 55 publications

(55 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Incubation under pressure was carried out in a pressure cell equipped with sapphire optical windows, similar to that originally described by Paladini and Weber (44,42). The temperature of the pressure cell was controlled by means of a jacket connected to a circulating bath.…”

Section: Methodsmentioning

confidence: 99%

“…On the contrary, denaturation by high pressure generally is a reversible process. Furthermore, high-pressure treatment can lead to dissociation of aggregated structures and may result in formation of monomers and natively folded structures (33,35,(41)(42)(43). Hence, in addition to cosolvent and temperature perturbation, pressure-dependent studies are able to shed new light on alternative folding-aggregation pathways and their intermediate states.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process

2008

View full text Add to dashboard Cite

Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance coupled with a progressive loss of insulin secretion that is associated with a decrease in pancreatic islet beta-cell mass and the deposition of amyloid in the extracellular matrix of beta-cells, which lead to islet cell death. The principal component of the islet amyloid is a pancreatic hormone called islet amyloid polypeptide (IAPP). High-pressure coupled with FT-IR spectroscopic and AFM studies were carried out to elucidate further information about the aggregation pathway as well as the aggregate structures of IAPP. To this end, a comparative fibrillation study of IAPP fragments was carried out as well. As high hydrostatic pressure (HHP) is acting to weaken or even prevent hydrophobic self-organization and electrostatic interactions, application of HHP has been used as a measure to reveal the importance of these interactions in the fibrillation process of IAPP and its fragments. IAPP preformed fibrils exhibit a strong polymorphism with heterogeneous structures, a large population of which are rather sensitive to high hydrostatic pressure, thus indicating a high percentage of ionic and hydrophobic interactions and loose packing of these species. Conversely, fragments 1-19 and 1-29 are resistant to pressure treatment, suggesting more densely packed aggregate structures with less void volume and strong cooperative hydrogen bonding. Furthermore, the FT-IR data indicate that fragment 1-29 has intermolecular beta-sheet conformational properties different from those of fragment 1-19, the latter exhibiting polymorphic behavior with more disordered structures and less strongly hydrogen bonded fibrillar assemblies. The data also suggest that hydrophobic interactions and/or less efficient packing of amino acids 30-37 region leads to the marked pressure sensitivity observed for full-length IAPP.

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process

2008

View full text Add to dashboard Cite

show abstract

Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis

Harris

Milton

2012

Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

View full text Add to dashboard Cite

In this chapter we provided the overall background to the subject of protein aggregation and fibrillogenesis in amyloidogenesis, with introduction and brief discussion of the various topics that are included with the coming chapters. The division of the book into basic science and clinical science sections enables correlation of the topics to be made. The many proteins and peptides that have currently been found to undergo fibrillogenesis are tabulated. A broad technical survey is made, to indicate the vast array of techniques currently available to study aspects of protein oligomerization, aggregation and fibrillogenesis. These are split into three groups and tabulated, as the microscopical techniques, the analytical and biophysical methods, and the biochemical and cellular techniques. A few techniques are discussed, but in most cases only a link to relevant recent literature is provided.

show abstract

Islet amyloid polypeptide and high hydrostatic pressure: towards an understanding of the fibrillization process

Cited by 2 publications

References 55 publications

Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process

Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process

Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis

Contact Info

Product

Resources

About