scholarly journals A Different hIAPP Polymorph Is Observed in Human Serum Than in Aqueous Buffer: Demonstration of a New Method for Studying Amyloid Fibril Structure Using Infrared Spectroscopy

2020 ◽  
Vol 11 (15) ◽  
pp. 6382-6388 ◽  
Author(s):  
Caitlyn R. Fields ◽  
Sidney S. Dicke ◽  
Megan K. Petti ◽  
Martin T. Zanni ◽  
Justin P. Lomont
Keyword(s):  
Infrared Spectroscopy ◽  
Human Serum ◽  
Amyloid Fibril ◽  
New Method ◽  
Aqueous Buffer ◽  
Fibril Structure

Highly sensitive and ratiometric luminescence sensing of heparin through templated cyanostilbene assemblies

The Analyst ◽  
2021 ◽  
Author(s):  
Shubhra Kanti Bhaumik ◽  
Supratim Banerjee
Keyword(s):  
Human Serum ◽  
Cluster Formation ◽  
Fluorometric Detection ◽  
Aqueous Buffer ◽  
Highly Sensitive

Heparin templated highly emissive cluster formation of di-cationic cyanostilbenes was utilized for the fluorometric detection of the polyanion in aqueous buffer, human serum and plasma.

A new method to classify amyloid fibril proteins

1985 ◽  
Vol 67 (3-4) ◽  
pp. 272-278 ◽  
Author(s):  
T. Kitamoto ◽  
J. Tateishi ◽  
K. Hikita ◽  
H. Nagara ◽  
I. Takeshita
Keyword(s):  
Amyloid Fibril ◽  
New Method

scholarly journals The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure

2020 ◽  
Author(s):  
Yunpeng Sun ◽  
Kun Zhao ◽  
Wencheng Xia ◽  
Jinge Gu ◽  
Yeyang Ma ◽  
...  
Keyword(s):  
Phase Separation ◽  
Nuclear Localization ◽  
Amyloid Fibril ◽  
Low Complexity ◽  
Nuclear Localization Sequence ◽  
Amyloid Aggregation ◽  
Dynamic Phase ◽  
Fibril Structure ◽  
Cytoplasmic Transport ◽  
Localization Sequence

AbstractHuman heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) serves as a key regulating protein in RNA metabolism. Malfunction of hnRNPA1 in nucleo-cytoplasmic transport or dynamic phase separation leads to abnormal amyloid aggregation and neurodegeneration. The low complexity (LC) domain of hnRNPA1 drives both dynamic phase separation and amyloid aggregation. Here, we use cryo-electron microscopy to determine the amyloid fibril structure formed by hnRNPA1 LC domain. Remarkably, the structure reveals that the nuclear localization sequence of hnRNPA1 (termed PY-NLS), which is initially known to mediate the nucleo-cytoplamic transport of hnRNPA1 through binding with karyopherin-β2 (Kapβ2), represents the major component of the fibril core. The residues that contribute to the binding of PY-NLS with Kapβ2 also exert key molecular interactions to stabilize the fibril structure. Notably, hnRNPA1 mutations found in familial amyotrophic lateral sclerosis (ALS) and multisystem proteinopathoy (MSP) are all involved in the fibril core and contribute to fibril stability. Our work illuminate structural understandings on the pathological amyloid aggregation of hnRNPA1 and the amyloid disaggregase activity of Kapβ2, and highlights the multiple roles of PY-NLS in hnRNPA1 homeostasis.

Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Structural Requirements ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Near-infrared spectroscopy as a new method for post-harvest monitoring of white truffles

2020 ◽  
Vol 19 (4) ◽  
pp. 329-337 ◽  
Author(s):  
Luisa Mandrile ◽  
Antonietta Mello ◽  
Alfredo Vizzini ◽  
Raffaella Balestrini ◽  
Andrea Mario Rossi
Keyword(s):  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Near Infrared ◽  
New Method ◽  
Post Harvest

scholarly journals Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor

2012 ◽  
Vol 4 (5) ◽  
pp. 355-360 ◽  
Author(s):  
Chris T. Middleton ◽  
Peter Marek ◽  
Ping Cao ◽  
Chi-cheng Chiu ◽  
Sadanand Singh ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Amyloid Fibril ◽  
Two Dimensional ◽  
Complex Behaviour ◽  
Two Dimensional Infrared Spectroscopy
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