Proanthocyanidin B2 attenuates postprandial blood glucose and its inhibitory effect on alpha-glucosidase: analysis by kinetics, fluorescence spectroscopy, atomic force microscopy and molecular docking

2018 ◽  
Vol 9 (9) ◽  
pp. 4673-4682 ◽  
Author(s):  
Lin Han ◽  
Lingling Zhang ◽  
Wenfang Ma ◽  
Ding Li ◽  
Rujie Shi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Docking ◽  
Blood Glucose ◽  
Fluorescence Spectroscopy ◽  
Inhibitory Effect ◽  
Postprandial Blood Glucose ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sucrose Loading ◽  
Alpha Glucosidase

As a dimer of proanthocyanidin, proanthocyanidin B2 (PB2) was found to effectively attenuate postprandial blood glucose in mice after sucrose loading.

scholarly journals Study of a Model Humic Acid-type Polymer by Fluorescence Spectroscopy and Atomic Force Microscopy

2012 ◽  
Vol 03 (07) ◽  
pp. 478-484
Author(s):  
Marcilene Ferrari Barriquello ◽  
Fábio de Lima Leite ◽  
Daiana Kotra Deda ◽  
Sérgio da Costa Saab ◽  
Nelson Consolin-Filho ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Humic Acid ◽  
Fluorescence Spectroscopy ◽  
Force Microscopy ◽  
Atomic Force ◽  
Acid Type

scholarly journals The Inhibitory Effect of Resveratrol on Elastin Amyloidogenesis

2014 ◽  
Vol 2014 ◽  
pp. 1-4
Author(s):  
Antonietta Pepe ◽  
Florian Delaunay ◽  
Angelo Bracalello ◽  
Brigida Bochicchio
Keyword(s):  
Molecular Structure ◽  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Inhibitory Effect ◽  
Degenerative Diseases ◽  
Force Microscopy ◽  
Atomic Force ◽  
Circular Dichroïsm

The role of polyphenols in the prevention of degenerative diseases is emerging in the last years. In this report, we will investigate in vitro the inhibitory effect of resveratrol on elastin amyloidogenesis. The effect of resveratrol on molecular structure was investigated by circular dichroism spectroscopy, while the inhibitory effect on self-assembly was evaluated by turbidimetry as a function of temperature and by atomic force microscopy.

scholarly journals Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Rona Banerjee
Keyword(s):  
Atomic Force Microscopy ◽  
Ftir Spectroscopy ◽  
Amyloid Beta ◽  
Inhibitory Effect ◽  
Amyloid Beta Peptide ◽  
Inhibitory Effects ◽  
Force Microscopy ◽  
Mononuclear Complexes ◽  
Atomic Force ◽  
Beta Peptide

Mononuclear complexes of Curcumin with Cu(II) and Zn(II) have been synthesized and, characterized and their effects on the fibrillization and aggregation of amyloid-beta (Aβ) peptide have been studied. FTIR spectroscopy and atomic force microscopy (AFM) observations demonstrate that the complexes can inhibit the transition from less structured oligomers toβ-sheet rich protofibrils which act as seeding factors for further fibrillization. The metal complexes also impart more improved inhibitory effects than Curcumin on peptide fibrillization.

scholarly journals DNA-Directed Assembly of Carbon Nanotube–Protein Hybrids

Biomolecules ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 955
Author(s):  
Mark Freeley ◽  
Rebecca E. A. Gwyther ◽  
D. Dafydd Jones ◽  
Matteo Palma
Keyword(s):  
Atomic Force Microscopy ◽  
Carbon Nanotube ◽  
Fluorescence Spectroscopy ◽  
Emission Intensity ◽  
Directed Assembly ◽  
Electronic Coupling ◽  
Force Microscopy ◽  
Controlled Assembly ◽  
Atomic Force ◽  
Microscopy Images

Here, we report the controlled assembly of SWCNT–GFP hybrids employing DNA as a linker. Two distinct, enriched SWCNTs chiralities, (6,5), (7,6), and an unsorted SWCNT solution, were selectively functionalized with DNA and hybridized to a complementary GFPDNA conjugate. Atomic force microscopy images confirmed that GFP attachment occurred predominantly at the terminal ends of the nanotubes, as designed. The electronic coupling of the proteins to the nanotubes was confirmed via in-solution fluorescence spectroscopy, that revealed an increase in the emission intensity of GFP when linked to the CNTs.

Inhibitory effect of aqueous extract from the gall of Rhus chinensis on alpha-glucosidase activity and postprandial blood glucose

2003 ◽  
Vol 85 (2-3) ◽  
pp. 283-287 ◽  
Author(s):  
Young-Jun Shim ◽  
Ho-Kyung Doo ◽  
Se-Young Ahn ◽  
Yong-Suk Kim ◽  
Je-Kyung Seong ◽  
...  
Keyword(s):  
Blood Glucose ◽  
Aqueous Extract ◽  
Inhibitory Effect ◽  
Postprandial Blood Glucose ◽  
Glucosidase Activity ◽  
Rhus Chinensis ◽  
Alpha Glucosidase

scholarly journals Effect of Varying Concentrations of Docosahexaenoic Acid on Amyloid Beta (1–42) Aggregation: An Atomic Force Microscopy Study

Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3089 ◽  
Author(s):  
Brenda Lee ◽  
Simon Attwood ◽  
Stephen Turnbull ◽  
Zoya Leonenko
Keyword(s):  
Atomic Force Microscopy ◽  
Docosahexaenoic Acid ◽  
Amyloid Beta ◽  
Amyloid Fibril ◽  
Inhibitory Effect ◽  
Fibril Formation ◽  
Force Microscopy ◽  
Atomic Force ◽  
Amyloid Fibril Formation ◽  
Fibril Length

Healthcare has advanced significantly, bringing with it longer life expectancies and a growing population of elders who suffer from dementia, specifically Alzheimer’s disease (AD). The amyloid beta (Aβ) peptide has been implicated in the cause of AD, where the peptides undergo a conformational change and form neurotoxic amyloid oligomers which cause neuronal cell death. While AD has no cure, preventative measures are being designed to either slow down or stop the progression of this neurodegenerative disease. One of these measures involves dietary supplements with polyunsaturated fatty acids such as docosahexaenoic acid (DHA). This omega-3 fatty acid is a key component of brain development and has been suggested to reduce the progression of cognitive decline. However, different studies have yielded different results as to whether DHA has positive, negative, or no effects on Aβ fibril formation. We believe that these discrepancies can be explained with varying concentrations of DHA. Here, we test the inhibitory effect of different concentrations of DHA on amyloid fibril formation using atomic force microscopy. Our results show that DHA has a strong inhibitory effect on Aβ1–42 fibril formation at lower concentrations (50% reduction in fibril length) than higher concentrations above its critical micelle concentration (70% increase in fibril length and three times the length of those at lower concentrations). We provide evidence that various concentrations of DHA can play a role in the inhibitory effects of amyloid fibril formation in vitro and help explain the discrepancies observed in previous studies.

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