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Molecules (Basel, Switzerland) Dec 2023Amylase is an indispensable hydrolase in insect growth and development. Its varied enzymatic parameters cause insects to have strong stress resistance. Amylase gene... (Review)
Review
Amylase is an indispensable hydrolase in insect growth and development. Its varied enzymatic parameters cause insects to have strong stress resistance. Amylase gene replication is a very common phenomenon in insects, and different copies of amylase genes enable changes in its location and function. In addition, the classification, structure, and interaction between insect amylase inhibitors and amylases have also invoked the attention of researchers. Some plant-derived amylase inhibitors have inhibitory activities against insect amylases and even mammalian amylases. In recent years, an increasing number of studies have clarified the effects of pesticides on the amylase activity of target and non-target pests, which provides a theoretical basis for exploring safe and efficient pesticides, while the exact lethal mechanisms and safety in field applications remain unclear. Here, we summarize the most recent advances in insect amylase studies, including its sequence and characteristics and the regulation of amylase inhibitors (α-AIs). Importantly, the application of amylases as the nanocide trigger, RNAi, or other kinds of pesticide targets will be discussed. A comprehensive foundation will be provided for applying insect amylases to the development of new-generation insect management tools and improving the specificity, stability, and safety of pesticides.
Topics: Animals; alpha-Amylases; Amylases; Enzyme Inhibitors; Insecta; Pest Control; Pesticides
PubMed: 38067617
DOI: 10.3390/molecules28237888 -
World Journal of Microbiology &... Dec 2023α-Amylases are essential biocatalysts representing a billion-dollar market with significant long-term global demand. They have varied applications ranging from... (Review)
Review
α-Amylases are essential biocatalysts representing a billion-dollar market with significant long-term global demand. They have varied applications ranging from detergent, textile, and food sectors such as bakery to, more recently, biofuel industries. Microbial α-amylases have distinct advantages over their plant and animal counterparts owing to generally good activities and better stability at temperature and pH extremes. With the scope of applications expanding, the need for new and improved α-amylases is ever-growing. However, scaling up microbial α-amylase technology from the laboratory to industry for practical applications is impeded by several issues, ranging from mass transfer limitations, low enzyme yields, and energy-intensive product recovery that adds to high production costs. This review highlights the major challenges and prospects for the production of microbial α-amylases, considering the various avenues of industrial bioprocessing such as culture-independent approaches, nutrient optimization, bioreactor operations with design improvements, and product down-streaming approaches towards developing efficient α-amylases with high activity and recyclability. Since the sequence and structure of the enzyme play a crucial role in modulating its functional properties, we have also tried to analyze the structural composition of microbial α-amylase as a guide to its thermodynamic properties to identify the areas that can be targeted for enhancing the catalytic activity and thermostability of the enzyme through varied immobilization or selective enzyme engineering approaches. Also, the utilization of inexpensive and renewable substrates for enzyme production to isolate α-amylases with non-conventional applications has been briefly discussed.
Topics: Animals; alpha-Amylases; Amylases; Temperature; Enzyme Stability
PubMed: 38114825
DOI: 10.1007/s11274-023-03821-y -
Journal of Oral Rehabilitation Nov 2023Some studies have shown burning mouth syndrome (BMS) as comorbid psychosocial and psychiatric disorders, and as well, pointed at stress as a major risk factor. (Meta-Analysis)
Meta-Analysis Review
BACKGROUND
Some studies have shown burning mouth syndrome (BMS) as comorbid psychosocial and psychiatric disorders, and as well, pointed at stress as a major risk factor.
OBJECTIVE
The aim of this meta-analysis was to answer the following question: 'Is there an association between BMS and stress, compared to healthy controls?'
METHODS
Two reviewers searched for the effect of stress in BMS and published on five main databases and three from the grey literature. Various questionnaires and biomarkers were analysed. Of the 2489 selected articles, 30 met the inclusion criteria. Studies englobed questionnaires, such as Perceived Stress Questionnaire, Lipp Stress Symptoms Inventory, Holmes-Rahe scale, Depression, Anxiety, and Stress Scale (DASS-21), Recent Experience Test; and various biomarkers, such as cortisol, opiorphin, IgA, α-amylase and interleukins.
RESULTS
In all studies with questionnaires, stress was significantly increased in the BMS group vs. control. Patients with BMS presented 25.73% higher cortisol levels, 28.17% higher IgA levels and 40.62% higher α-amylase levels than controls. Meta-analysis found that BMS subjects presented 3.01 nmoL/L [0.53; 5.50] higher cortisol levels, 84.35 kU/L [15.00; 153.71] higher α-amylase levels, 29.25 mg/mL [9.86; 48.64] higher IgA levels and 258.59 pg/mL [59.24; 457.94] higher IL-8 levels than control. No differences were found for opiorphin concentration in ng/mL [-0.96; 2.53]. For interleukins, no differences were founded for IL-1 β, IL-2, IL-4, IL-6, IL-8, IL-10 and TNF-α.
CONCLUSION
Based on the available evidence, this meta-analysis suggests more stress factors in questionnaire-based studies, and higher levels of cortisol, α-amylase, IgA and IL-8 biomarkers in BMS subjects than controls.
Topics: Humans; Burning Mouth Syndrome; Hydrocortisone; Interleukin-8; alpha-Amylases; Biomarkers; Immunoglobulin A
PubMed: 37332081
DOI: 10.1111/joor.13536 -
Future Medicinal Chemistry Aug 2023Researchers seeking new drug candidates to treat diabetes mellitus have been exploring bioactive molecules found in nature, particularly tetrahydropyridines (THPs). A...
Researchers seeking new drug candidates to treat diabetes mellitus have been exploring bioactive molecules found in nature, particularly tetrahydropyridines (THPs). A library of THPs () were synthesized via a one-pot multicomponent reaction and investigated for their inhibition potential against α-glucosidase and α-amylase enzymes. A nitrophenyl-substituted compound with IC values of 0.15 ± 0.01 and 1.10 ± 0.04 μM, and a value of 1.30 mg/ml was identified as the most significant α-glucosidase and α-amylase inhibitor, respectively. Kinetic studies revealed the competitive mode of inhibition, and docking studies revealed that compound binds to the enzyme by establishing hydrophobic and hydrophilic interactions and a salt bridge interaction with His279. These molecules may be a potential drug candidate for diabetes in the future.
Topics: Humans; alpha-Amylases; alpha-Glucosidases; Diabetes Mellitus; Glycoside Hydrolase Inhibitors; Kinetics; Molecular Docking Simulation; Structure-Activity Relationship
PubMed: 37650736
DOI: 10.4155/fmc-2023-0073 -
International Journal of Molecular... Nov 2023α-Amylase is a generally acknowledged molecular target of a distinct class of antidiabetic drugs named α-glucosidase inhibitors. This class of medications is scarce... (Review)
Review
α-Amylase is a generally acknowledged molecular target of a distinct class of antidiabetic drugs named α-glucosidase inhibitors. This class of medications is scarce and rather underutilized, and treatment with current commercial drugs is accompanied by unpleasant adverse effects. However, mammalian α-amylase inhibitors are abundant in nature and form an extensive pool of high-affinity ligands that are available for drug discovery. Individual compounds and natural extracts and preparations are promising therapeutic agents for conditions associated with impaired starch metabolism, e.g., diabetes mellitus, obesity, and other metabolic disorders. This review focuses on the structural diversity and action mechanisms of active natural products with inhibitory activity toward mammalian α-amylases, and emphasizes proteinaceous inhibitors as more effective compounds with significant potential for clinical use.
Topics: Animals; Humans; alpha-Amylases; Hypoglycemic Agents; Glycoside Hydrolase Inhibitors; Metabolic Diseases; alpha-Glucosidases; Plant Extracts; Mammals
PubMed: 38003703
DOI: 10.3390/ijms242216514 -
Journal of Molecular Recognition : JMR Nov 2023Diabetes mellitus is one of the most critical health problems affecting the quality of life of people worldwide, especially in developing countries. According to the...
Diabetes mellitus is one of the most critical health problems affecting the quality of life of people worldwide, especially in developing countries. According to the World Health Organization reports, the number of patients with diabetes is approximately 420 million, and this number is estimated to be 642 million in 2040. There are 2 main types of diabetes: Type 1 (T1DM), where the body cannot produce enough insulin, and Type 2 (T2DM), where the body cannot use insulin properly. Patients with T1DM are treated with insulin injections while oral glucose-lowering drugs are used for patients with T2DM. Oral antihyperglycemic drugs used in the treatment of type 2 diabetes mellitus have different mechanisms. Among these, α-Glucosidase and α-amylase inhibitors are one of the most important inhibitors. The antidiabetic effect of the chalcones, which show rich activity, draws attention. This research aims to synthesize chalcone derivatives that could show potential antidiabetic activity. In this study, the inhibitory activity of the chalcone compounds (4a-4g, 5a-5g) was tested against α-glucosidase and α-amylase enzymes. Besides, molecular modeling was utilized to predict potential interactions of the synthesized compounds that exhibit inhibitory effects. In both in vitro and in silico studies, the analyses revealed that compound 5e exhibits strong inhibitory effects against α-glucosidase enzymes (Binding energy: -7.75 kcal/mol, IC : 28.88 μM). Additionally, compound 4f demonstrates encouraging inhibitory effects against α-Amylase (Binding energy: -11.08 kcal/mol, IC : 46. 21 μM).
Topics: Humans; alpha-Amylases; alpha-Glucosidases; Chalcone; Chalcones; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Glycoside Hydrolase Inhibitors; Hypoglycemic Agents; Insulin; Molecular Docking Simulation; Quality of Life
PubMed: 37720970
DOI: 10.1002/jmr.3061 -
Natural Product Research 2023One new compound, 4,7-dihydroxy-2-hydroxymethyl-5,6-dimethoxyanthraquinone (), along with eight known compounds (-) were isolated from the methanol extracts of the...
One new compound, 4,7-dihydroxy-2-hydroxymethyl-5,6-dimethoxyanthraquinone (), along with eight known compounds (-) were isolated from the methanol extracts of the aerial parts of (Lam.) K. Larsen. Their chemical structure was determined based on spectroscopic data interpretation and comparison with the reported data. The inhibitory effects of them on -amylase and -glucosidase were performed. The results showed that compounds , , , and against potent -glucosidase with the inhibition values of 98.14 ± 0.05, 98.19 ± 0.04, 97.01 ± 0.49, 84.43 ± 0.6% at 50 M, respectively. Compounds and displayed significance against -amylase at 200 M with inhibition values of 22.35 ± 1.10 and 60.47 ± 0.91%.
Topics: Glycoside Hydrolase Inhibitors; Hypoglycemic Agents; Chamaecrista; alpha-Glucosidases; alpha-Amylases; Plant Extracts; Plant Components, Aerial
PubMed: 36661236
DOI: 10.1080/14786419.2023.2169864 -
Journal of Agricultural and Food... Nov 2023A novel antidiabetic glycoprotein (PG) was isolated and purified from , and its structure and inhibiting activity on α-amylase and α-glucosidase were analyzed. The...
A novel antidiabetic glycoprotein (PG) was isolated and purified from , and its structure and inhibiting activity on α-amylase and α-glucosidase were analyzed. The purity of the PG was 95.29 ± 0.21%, and its molecular weight was 163.024 ± 5.55 kDa. The PG had a tetramer structure with α- and β-subunits, and it contained 54.12 ± 0.86% protein (with highly hydrophobic amino acids) and 41.19% ± 0.64% carbohydrate (composed of galactose). The PG was linked via an O-glycosidic bond, exhibiting an α-helical structure and high stability. In addition, the PG inhibited the activities of α-amylase and α-glucosidase, by changing the enzyme's structure toward the PG's structure in a noncompetitive inhibition mode. Molecular docking results showed that the PG inhibited α-amylase activity by hydrophobic interaction, whereas it inhibited α-glucosidase activity by hydrogen bonds and hydrophobic interaction. Overall, the PG was linked to polysaccharides via O-glycosidic bonds, showing an α-helical configuration and a hydrophobic effect, which altered the configuration of α-amylase and α-glucosidase and exerted hypoglycemic activity. This study provides insights into analyzing the structure and antidiabetic activity of glycoproteins.
Topics: Hypoglycemic Agents; Porphyra; alpha-Glucosidases; Molecular Docking Simulation; alpha-Amylases; Glycoproteins; Glycoside Hydrolase Inhibitors
PubMed: 37877414
DOI: 10.1021/acs.jafc.3c04276 -
Phytochemistry Dec 2023Eleven previously undescribed lignan constituents, including five 8-O-4' type neolignans, viburnurcosides A-E (1-5), three benzofuran type neolignans, viburnurcosides...
Eleven previously undescribed lignan constituents, including five 8-O-4' type neolignans, viburnurcosides A-E (1-5), three benzofuran type neolignans, viburnurcosides F-H (6-8), and three tetrahydrofuran type lignans, viburnurcosides I-K (9-11), were isolated from the fruits of Viburnum urceolatum. The structures of all isolates were elucidated by an extensive analysis of the NMR and HRESIMS data. The absolute configurations of these compounds were determined by quantum-chemical electronic circular dichroism calculation and comparison. The sugar units of viburnurcosides A-K were identified by acid hydrolysis and HPLC analysis of the chiral derivatives of monosaccharides. The in vitro enzyme inhibition assay exhibited that viburnurcoside J (10) had the most potent inhibitory activity against α-amylase and α-glucosidase with the IC values of 19.75 and 9.14 μM, respectively, which were stronger than those of the positive control acarbose (37.31 and 26.75 μM, respectively). The potential binding modes of viburnurcoside J (10) with α-amylase and α-glucosidase were also analyzed by molecular modeling.
Topics: alpha-Glucosidases; alpha-Amylases; Viburnum; Fruit; Molecular Structure; Glycoside Hydrolase Inhibitors; Lignans
PubMed: 37827226
DOI: 10.1016/j.phytochem.2023.113895