An Insight of Alpha-amylase Inhibitors as a Valuable Tool in the Management of Type 2 Diabetes Mellitus
Copyright© Bentham Science Publishers; For any queries, please email at epubbenthamscience.net..
BACKGROUND: Among the millions of people around the world, the most prevalent metabolic disorder is diabetes mellitus. Due to the drawbacks which are associated with commercially available antidiabetic agents, new therapeutic approaches are needed to be considered. Alpha-amylase is a membrane- bound enzyme which is responsible for the breakdown of polysaccharides such as starch to monosaccharides which can be absorbed.
METHODS: We searched the scientific database using alpha-amylase, diabetes, antidiabetic agents as the keywords. Here in, only peer-reviewed research articles were collected which were useful to our current work.
RESULTS: To overcome the research gap, the alpha-amylase enzyme is regarded as a good target for antidiabetic agents to design the drug and provide an alternate approach for the treatment of type 2 diabetes mellitus. Basically, alpha-amylase inhibitors are classified into two groups: proteinaceous inhibitors, and non-proteinaceous inhibitors. Recently, non-proteinaceous inhibitors are being explored which includes chalcones, flavones, benzothiazoles, etc. as the potential antidiabetic agents.
CONCLUSION: Herein, we discuss various potential antidiabetic agents which are strategically targeted alpha-amylase enzyme. These are having lesser side effects as compared to other antidiabetic agents, and are proposed to prevent the digestion and absorption of glucose leading to a decrease in the blood glucose level.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2020 |
|---|---|
| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:16 |
|---|---|
| Enthalten in: |
Current diabetes reviews - 16(2020), 2 vom: 02., Seite 117-136 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Bashary, Roqia [VerfasserIn] |
|---|
| Links: |
|---|
| Themen: |
Alpha-Amylases |
|---|
| Anmerkungen: |
Date Completed 17.02.2020 Date Revised 17.02.2020 published: Print Citation Status MEDLINE |
|---|
| doi: |
10.2174/1573399815666190618093315 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM29851351X |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM29851351X | ||
| 003 | DE-627 | ||
| 005 | 20231225094329.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.2174/1573399815666190618093315 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0995.xml |
| 035 | |a (DE-627)NLM29851351X | ||
| 035 | |a (NLM)31237215 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Bashary, Roqia |e verfasserin |4 aut | |
| 245 | 1 | 3 | |a An Insight of Alpha-amylase Inhibitors as a Valuable Tool in the Management of Type 2 Diabetes Mellitus |
| 264 | 1 | |c 2020 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 17.02.2020 | ||
| 500 | |a Date Revised 17.02.2020 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright© Bentham Science Publishers; For any queries, please email at epubbenthamscience.net. | ||
| 520 | |a BACKGROUND: Among the millions of people around the world, the most prevalent metabolic disorder is diabetes mellitus. Due to the drawbacks which are associated with commercially available antidiabetic agents, new therapeutic approaches are needed to be considered. Alpha-amylase is a membrane- bound enzyme which is responsible for the breakdown of polysaccharides such as starch to monosaccharides which can be absorbed | ||
| 520 | |a METHODS: We searched the scientific database using alpha-amylase, diabetes, antidiabetic agents as the keywords. Here in, only peer-reviewed research articles were collected which were useful to our current work | ||
| 520 | |a RESULTS: To overcome the research gap, the alpha-amylase enzyme is regarded as a good target for antidiabetic agents to design the drug and provide an alternate approach for the treatment of type 2 diabetes mellitus. Basically, alpha-amylase inhibitors are classified into two groups: proteinaceous inhibitors, and non-proteinaceous inhibitors. Recently, non-proteinaceous inhibitors are being explored which includes chalcones, flavones, benzothiazoles, etc. as the potential antidiabetic agents | ||
| 520 | |a CONCLUSION: Herein, we discuss various potential antidiabetic agents which are strategically targeted alpha-amylase enzyme. These are having lesser side effects as compared to other antidiabetic agents, and are proposed to prevent the digestion and absorption of glucose leading to a decrease in the blood glucose level | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Review | |
| 650 | 4 | |a Diabetes | |
| 650 | 4 | |a alpha-amylase | |
| 650 | 4 | |a alpha-amylase inhibitor | |
| 650 | 4 | |a antidiabetic agents | |
| 650 | 4 | |a hyperglycemia | |
| 650 | 4 | |a hypoglycemia. | |
| 650 | 7 | |a Blood Glucose |2 NLM | |
| 650 | 7 | |a Enzyme Inhibitors |2 NLM | |
| 650 | 7 | |a Hypoglycemic Agents |2 NLM | |
| 650 | 7 | |a alpha-Amylases |2 NLM | |
| 650 | 7 | |a EC 3.2.1.1 |2 NLM | |
| 700 | 1 | |a Vyas, Manish |e verfasserin |4 aut | |
| 700 | 1 | |a Nayak, Surendra Kumar |e verfasserin |4 aut | |
| 700 | 1 | |a Suttee, Ashish |e verfasserin |4 aut | |
| 700 | 1 | |a Verma, Surajpal |e verfasserin |4 aut | |
| 700 | 1 | |a Narang, Rakesh |e verfasserin |4 aut | |
| 700 | 1 | |a Khatik, Gopal L |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Current diabetes reviews |d 2005 |g 16(2020), 2 vom: 02., Seite 117-136 |w (DE-627)NLM177100095 |x 1875-6417 |7 nnns |
| 773 | 1 | 8 | |g volume:16 |g year:2020 |g number:2 |g day:02 |g pages:117-136 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.2174/1573399815666190618093315 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 16 |j 2020 |e 2 |b 02 |h 117-136 | ||