Capabilities of MS for Analytical Quantitative Determination of the Ratio of α- and βAsp7 Isoforms of the Amyloid-β Peptide in Binary Mixtures

2011 ◽  
Vol 83 (8) ◽  
pp. 3205-3210 ◽  
Author(s):  
Maria I. Indeykina ◽  
Igor A. Popov ◽  
Sergey A. Kozin ◽  
Alexey S. Kononikhin ◽  
Oleg N. Kharybin ◽  
...  
Keyword(s):  
Quantitative Determination ◽  
Binary Mixtures ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Evaluation of MALDI-TOF/TOF Mass Spectrometry Approach for Quantitative Determination of Aspartate Residue Isomerization in the Amyloid-β Peptide

2019 ◽  
Vol 30 (7) ◽  
pp. 1325-1329 ◽  
Author(s):  
Stanislav I. Pekov ◽  
Daniil G. Ivanov ◽  
Anna E. Bugrova ◽  
Maria I. Indeykina ◽  
Natalia V. Zakharova ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Determination ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Maldi Tof ◽  
Aspartate Residue

scholarly journals Zn2+ Interaction with Amyloid-Β: Affinity and Speciation

Molecules ◽  
2019 ◽  
Vol 24 (15) ◽  
pp. 2796 ◽  
Author(s):  
Arena ◽  
Rizzarelli
Keyword(s):  
Species Distribution ◽  
Multiple Equilibria ◽  
Amyloid Β ◽  
Data Interpretation ◽  
Amyloid Β Peptide ◽  
Experimental Conditions ◽  
Pros And Cons ◽  
The Stability ◽  
Ph Range

Conflicting values, obtained by different techniques and often under different experimental conditions have been reported on the affinity of Zn2+ for amyloid-β, that is recognized as the major interaction responsible for Alzheimer’s disease. Here, we compare the approaches employed so far, i.e., the evaluation of Kd and the determination of the stability constants to quantitatively express the affinity of Zn2+ for the amyloid-β peptide, evidencing the pros and cons of the two approaches. We also comment on the different techniques and conditions employed that may lead to divergent data. Through the analysis of the species distribution obtained for two selected examples, we show the implications that the speciation, based on stoichiometric constants rather than on Kd, may have on data interpretation. The paper also demonstrates that the problem is further complicated by the occurrence of multiple equilibria over a relatively narrow pH range.

Colorimetric determination of amyloid-β peptide using MOF-derived nanozyme based on porous ZnO-Co3O4 nanocages

2021 ◽  
Vol 188 (2) ◽  
Author(s):  
Xi Zhou ◽  
Shuangling Wang ◽  
Cong Zhang ◽  
Yulong Lin ◽  
Jie Lv ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Colorimetric Determination ◽  
Amyloid Β Peptide

Simultaneous Determination of Flavor Enhancers Inosine 5´-Monophosphate and Guanosine 5´-Monophosphate in Food Preparations by Derivative Spectrophotometry

1993 ◽  
Vol 76 (4) ◽  
pp. 754-759 ◽  
Author(s):  
Isabel Durán-Merás ◽  
Francisco Salinas ◽  
Arsenio Muńoz de la Peńa ◽  
Miguel Lopez Rόsas
Keyword(s):  
Quantitative Determination ◽  
Simultaneous Determination ◽  
Absorption Spectra ◽  
Binary Mixtures ◽  
Monosodium Glutamate ◽  
Derivative Spectrophotometry ◽  
First Derivative ◽  
First Derivative Spectrophotometry

Abstract A derivative spectrophotometry method was developed for the quantitative determination of 2 flavor enhancers, inosine 5´-monophosphate (IMP) and guanosine 5´monophosphate (GMP), in the presence of monosodium glutamate (MSG). Procedures for determining IMP and GMP singly and in binary mixtures are described. Overlapping absorption spectra of both compounds were resolved by using first-derivative spectrophotometry. By measuring the first-derivative signals of IMP and GMP at 253 and 248 nm, respectively, simultaneous determination was possible for IMP and GMP at 5–40 μg/mL, in the presence of up to 5000 μg/mL MSG. The method was satisfactorily used to determine IMP and GMP in several food preparations.

Amyloid β-peptide and Alzheimer's disease

2014 ◽  
Vol 56 ◽  
pp. 99-110 ◽  
Author(s):  
David Allsop ◽  
Jennifer Mayes
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Senile Plaques ◽  
Strong Support ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Cascade Hypothesis ◽  
Sequence Of Events ◽  
Aβ Amyloid ◽  
Amyloid Cascade

One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

Sign in / Sign up

Export Citation Format

Share Document