scholarly journals Amylin Proprotein Processing Generates Progressively More Amyloidogenic Peptides that Initially Sample the Helical State†

Biochemistry ◽  
2008 ◽  
Vol 47 (37) ◽  
pp. 9900-9910 ◽  
Author(s):  
Isaac T. Yonemoto ◽  
Gerard J. A. Kroon ◽  
H. Jane Dyson ◽  
William E. Balch ◽  
Jeffery W. Kelly
Keyword(s):  
Helical State ◽  
Proprotein Processing ◽  
Amyloidogenic Peptides

scholarly journals Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus

2020 ◽  
Vol 21 (17) ◽  
pp. 6382 ◽  
Author(s):  
Stanislav Kurpe ◽  
Sergei Grishin ◽  
Alexey Surin ◽  
Olga Selivanova ◽  
Roman Fadeev ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Thermus Thermophilus ◽  
Antibacterial Properties ◽  
Cell Penetration ◽  
Research Directions ◽  
Bacterial Proteins ◽  
Hiv Transcription ◽  
Parent Protein ◽  
Amyloidogenic Peptides ◽  
New Research

Controlling the aggregation of vital bacterial proteins could be one of the new research directions and form the basis for the search and development of antibacterial drugs with targeted action. Such approach may be considered as an alternative one to antibiotics. Amyloidogenic regions can, like antibacterial peptides, interact with the “parent” protein, for example, ribosomal S1 protein (specific only for bacteria), and interfere with its functioning. The aim of the work was to search for peptides based on the ribosomal S1 protein from T. thermophilus, exhibiting both aggregation and antibacterial properties. The biological system of the response of Gram-negative bacteria T. thermophilus to the action of peptides was characterized. Among the seven studied peptides, designed based on the S1 protein sequence, the R23I (modified by the addition of HIV transcription factor fragment for bacterial cell penetration), R23T (modified), and V10I (unmodified) peptides have biological activity that inhibits the growth of T. thermophilus cells, that is, they have antimicrobial activity. But, only the R23I peptide had the most pronounced activity comparable with the commercial antibiotics. We have compared the proteome of peptide-treated and intact T. thermophilus cells. These important data indicate a decrease in the level of energy metabolism and anabolic processes, including the processes of biosynthesis of proteins and nucleic acids. Under the action of 20 and 50 μg/mL R23I, a decrease in the number of proteins in T. thermophilus cells was observed and S1 ribosomal protein was absent. The obtained results are important for understanding the mechanism of amyloidogenic peptides with antimicrobial activity and can be used to develop new and improved analogues.

scholarly journals Developmental expression of proprotein-processing endoprotease furin in rat pancreatic islets.

Endocrinology ◽  
1996 ◽  
Vol 137 (11) ◽  
pp. 5126-5134 ◽  
Author(s):  
T Kayo ◽  
Y Konda ◽  
S Tanaka ◽  
K Takata ◽  
A Koizumi ◽  
...  
Keyword(s):  
Pancreatic Islets ◽  
Developmental Expression ◽  
Rat Pancreatic Islets ◽  
Proprotein Processing

scholarly journals A New Fluorescence Probe for Rapid Detection of Amyloid

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Vivek Shinh Kshtriya ◽  
Bharti Koshti ◽  
Shradhey Gupta ◽  
khashti Ballabh Joshi ◽  
...  
Keyword(s):  
Rapid Detection ◽  
Control Experiment ◽  
Fluorescence Probe ◽  
Photophysical Properties ◽  
Cost Effective ◽  
The Novel ◽  
High Quantum Yield ◽  
Turn On ◽  
Heat Treated ◽  
Amyloidogenic Peptides

<p>We report efficient synthesis and photophysical properties of a novel fluorescent pyridothiazole based construct by a facile methodology and its application as a sensor for rapid, selective as well as sensitive detection of amyloid fibres. The novel compound has exceptionally high quantum yield and sensitivity. The fluorescence of pyridothiazole construct is completely quenched (Turn-OFF) upon addition of cupric ions and the fluorescence is recovered on addition of amyloidogenic peptides like A<i>β</i><sub>42 </sub>(Turn-ON). The control experiment with native and heat treated BSA suggest that the new probe binds to beeta/<i>β</i> sheets present in amyloid. The new probe offers direct visualization of fluorescence ‘Turn-OFF’ ‘Turn-ON’ under long UV without the use of sophisticated instrumentation. Hence, a very simple, facile and cost-effective methodology for the rapid detection of amyloid is presented and it may in all possibility pave the way for the design of a better probe for sensing amyloids than conventional ThT.</p>

scholarly journals Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation

Prion ◽  
2013 ◽  
Vol 7 (2) ◽  
pp. 175-184 ◽  
Author(s):  
Evgeny E. Bezsonov ◽  
Minna Groenning ◽  
Oxana V. Galzitskaya ◽  
Anton A. Gorkovskii ◽  
Gennady V. Semisotnov ◽  
...  
Keyword(s):  
Cell Wall ◽  
Yeast Cell ◽  
Fibril Formation ◽  
Yeast Cell Wall ◽  
Amyloidogenic Peptides ◽  
Ph Dependent

Mechanisms of Membrane Pore Formation by Amyloidogenic Peptides in Amyotrophic Lateral Sclerosis

2016 ◽  
Vol 22 (29) ◽  
pp. 9958-9961 ◽  
Author(s):  
Charles H. Chen ◽  
Ayesha Khan ◽  
Joseph Jen-Tse Huang ◽  
Martin B. Ulmschneider
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Pore Formation ◽  
Membrane Pore ◽  
Amyloidogenic Peptides ◽  
Lateral Sclerosis
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