Results 111 to 120 of about 146,148 (156)
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Structure-activity relationships and the underlying mechanism of α-amylase inhibition by hyperoside and quercetin: Multi-spectroscopy and molecular docking analyses.

Spectrochimica Acta Part A - Molecular and Biomolecular Spectroscopy, 2022
Inhibiting the activity of α-amylase has been considered an effective strategy to manage hyperglycemia. Hyperoside and quercetin are the main natural flavonoids in various plants, and the inhibition mechanism on α-amylase remains unclear.
Heyu Shen   +7 more
semanticscholar   +1 more source

Arylureidoaurones: Synthesis, in vitro α-glucosidase, and α-amylase inhibition activity.

Bioorganic chemistry (Print), 2023
Because of the colossal global burden of diabetes, there is an urgent need for more effective and safer drugs. We designed and synthesized a new series of aurone derivatives possessing phenylureido or bis-phenylureido moieties as α-glucosidase and α ...
Mohammad Kazempour-Dizaji   +5 more
semanticscholar   +1 more source

α-Amylase inhibition, cytotoxicity and influence of the in vitro gastrointestinal digestion on the bioaccessibility of phenolic compounds in the peel and seed of Theobroma grandiflorum.

Food Chemistry, 2021
The aim of this work was to evaluate the bioaccessibility, cytotoxicity, antioxidant and antidiabetic potential of peel and seeds of cupuassu (Theobroma grandiflorum).
J. Andrade   +6 more
semanticscholar   +1 more source

Solvent Effect on Phenolic Compounds Extraction, Antioxidant Capacities and Α-Amylase and Α-Glucosidase Inhibition of Clematis flammula and Periploca angustifolia

Journal of Pharmaceutics & Drug Delivery Research, 2016
Solvent Effect on Phenolic Compounds Extraction, Antioxidant Capacities and Α-Amylase and Α-Glucosidase Inhibition of Clematis flammula and Periploca angustifolia Abstract Phytochemicals are extensively found at different levels in many medicinal plants.
Khaled Athmouni, Taheni Belghith
openaire   +1 more source

Phytochemical profile, antioxidant, α-amylase inhibition, binding interaction and docking studies of Justicia carnea bioactive compounds with α-amylase.

Biophysical Chemistry, 2020
The present study investigated the antioxidant and invitro antidiabetic capacities of Justicia carnea aqueous leaf extract (JCAE) using α-amylase inhibition model.
A. Anigboro   +4 more
semanticscholar   +1 more source

C-glucosidic ellagitannins and galloylated glucoses as potential functional food ingredients with anti-diabetic properties: a study of α-glucosidase and α-amylase inhibition.

Food Chemistry, 2019
Diabetes mellitus is a metabolic disorder characterized by hyperglycemia, which can be counteracted by inhibition of α-glucosidase and α-amylase, both involved in the carbohydrate metabolism.
N. Cardullo   +7 more
semanticscholar   +1 more source

Synthesis, crystal structures, computational studies and α-amylase inhibition of three novel 1,3,4-oxadiazole derivatives

, 2020
Oxadiazoles have broad range of biological applications and have been investigated widely by the scientific community. In this study, we report the synthesis, X-ray diffraction, density functional theory (DFT) and α-amylase inhibition activities of three
S. S. Hamdani   +6 more
semanticscholar   +1 more source

Kinetic of α-amylase inhibition by Gracilaria corticata and Sargassum angustifolium extracts and zinc oxide nanoparticles

, 2020
In this research, Gracilaria corticata red algae and Sargassum angustifolium brown algae were collected from tidal zones of the coastal areas of Bushehr (Persian Gulf coastline), and were extracted with methanol, ethanol, and sodium phosphate buffer ...
Soudeh Bahramian Nasab   +2 more
semanticscholar   +1 more source

Benzimidazole derivatives as potent α-amylase inhibitors: synthesis, characterization and in vitro α-amylase inhibition.

Future Medicinal Chemistry
AIM This study aims to evaluate the α-amylase inhibitory potential of newly synthesized benzimidazole derivatives, assessing their viability as prospective antidiabetic agents.
S. Kangad   +5 more
semanticscholar   +1 more source

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