Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR

1991 ◽  
Vol 113 (17) ◽  
pp. 6701-6703 ◽  
Author(s):  
Kurt J. Halverson ◽  
Irving Sucholeiki ◽  
Ted T. Ashburn ◽  
Peter T. Lansbury
Keyword(s):  
Sheet Forming ◽  
Beta Sheet ◽  
Amyloid Proteins

Beta-Sheet-Forming, Self-Assembled Peptide Nanomaterials towards Optical, Energy, and Healthcare Applications

Small ◽  
2015 ◽  
Vol 11 (30) ◽  
pp. 3623-3640 ◽  
Author(s):  
Sungjin Kim ◽  
Jae Hong Kim ◽  
Joon Seok Lee ◽  
Chan Beum Park
Keyword(s):  
Sheet Forming ◽  
Beta Sheet ◽  
Healthcare Applications ◽  
Optical Energy ◽  
Self Assembled

A Thermodynamic Scale for the .beta.-Sheet Forming Tendencies of the Amino Acids

Biochemistry ◽  
1994 ◽  
Vol 33 (18) ◽  
pp. 5510-5517 ◽  
Author(s):  
Catherine K. Smith ◽  
Jane M. Withka ◽  
Lynne Regan
Keyword(s):  
Amino Acids ◽  
Sheet Forming ◽  
Beta Sheet ◽  
Thermodynamic Scale

Chemical Catalyst-Promoted Photooxygenation of Amyloid Proteins

2021 ◽  
Author(s):  
Youhei Sohma ◽  
Taka Sawazaki ◽  
Motomu Kanai
Keyword(s):  
Higher Order ◽  
Misfolded Proteins ◽  
Beta Sheet ◽  
Amyloid Proteins ◽  
Aggregation Processes ◽  
Order Structures

Misfolded proteins produce aberrant fibrillar aggregates, called amyloid, that contain cross-beta-sheet higher order structures. The species generated in the aggregation processes (i.e., oligomers, protofibrils, and fibrils) are cytotoxic and can...

Role of the Structural Characteristics of Dendrimers in the Manifestation of the Antiamyloid Properties

INEOS OPEN ◽  
2020 ◽  
Vol 3 ◽  
Author(s):  
S. A. Sorokina ◽  
◽  
Yu. Yu. Stroilova ◽  
V. I. Muronets ◽  
Z. B. Shifrina ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Structural Characteristics ◽  
Short Review ◽  
External Factors ◽  
Amyloid Aggregation ◽  
Amyloid Proteins ◽  
Molecular Parameters ◽  
Amyloid Aggregates ◽  
Aggregation Processes

Among the compounds able to efficiently inhibit the amyloid aggregation of proteins and decompose the amyloid aggregates that cause neurodegenerative diseases, of particular interest are dendrimers, which represent individual macromolecules with the hypercrosslinked architectures and given molecular parameters. This short review outlines the peculiarities of the antiamyloid activity of dendrimers and discusses the effect of dendrimer structures and external factors on their antiamyloid properties. The potential of application of dendrimers in further investigations on the aggregation processes of amyloid proteins as the compounds that exhibit the remarkable antiamyloid activity is evaluated.

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