Cytotoxic effect, enzyme inhibition, and in silico studies of some novel N-substituted sulfonyl amides incorporating 1,3,4-oxadiazol structural motif
The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and h CAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and antiobesity antiepileptic, anticancer, antiinfective, antiglaucoma, and diuretic effects. Here, it has been attempted to discover novel multi...
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Published in | Molecular diversity Vol. 26; no. 5; pp. 2825 - 2845 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
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Springer International Publishing
01.10.2022
Springer Nature B.V |
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Abstract | The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and
h
CAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and antiobesity antiepileptic, anticancer, antiinfective, antiglaucoma, and diuretic effects. Here, it has been attempted to discover novel multi-target AChEIs and
h
CAIs that are highly potent, orally bioavailable, may be brain penetrant, and have higher effectiveness at lower doses than tacrine and acetazolamide. After detailed investigations both in vitro and in silico, novel
N
-substituted sulfonyl amide derivatives (
6a–j
) were determined to be highly potent inhibitors for AChE and
h
CAs (
K
I
s are in the range of 23.11–52.49 nM, 18.66–59.62 nM, and 9.33–120.80 nM for AChE,
h
CA I, and
h
CA II, respectively). Moreover, according to the cytotoxic effect studies, such as the ADME-Tox, cortex neuron cells, and neuroblastoma SH-SY5Y cell line, compounds
6a
,
6d
, and
6h
, which are the most potent representative versus the target enzymes, were identified as orally bioavailable, highly selective, and brain preferentially distributed AChEIs and
h
CAIs. The docking studies revealed precise binding modes between
6a
,
6d
, and
6h
and
h
CA II,
h
CA I, and AChE, respectively. The results presented here might provide a solid basis for further investigation into more potent AChEIs and
h
CAIs.
Graphical abstract |
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AbstractList | The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and hCAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and antiobesity antiepileptic, anticancer, antiinfective, antiglaucoma, and diuretic effects. Here, it has been attempted to discover novel multi-target AChEIs and hCAIs that are highly potent, orally bioavailable, may be brain penetrant, and have higher effectiveness at lower doses than tacrine and acetazolamide. After detailed investigations both in vitro and in silico, novel N-substituted sulfonyl amide derivatives (6a–j) were determined to be highly potent inhibitors for AChE and hCAs (KIs are in the range of 23.11–52.49 nM, 18.66–59.62 nM, and 9.33–120.80 nM for AChE, hCA I, and hCA II, respectively). Moreover, according to the cytotoxic effect studies, such as the ADME-Tox, cortex neuron cells, and neuroblastoma SH-SY5Y cell line, compounds 6a, 6d, and 6h, which are the most potent representative versus the target enzymes, were identified as orally bioavailable, highly selective, and brain preferentially distributed AChEIs and hCAIs. The docking studies revealed precise binding modes between 6a, 6d, and 6h and hCA II, hCA I, and AChE, respectively. The results presented here might provide a solid basis for further investigation into more potent AChEIs and hCAIs. The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and h CAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and antiobesity antiepileptic, anticancer, antiinfective, antiglaucoma, and diuretic effects. Here, it has been attempted to discover novel multi-target AChEIs and h CAIs that are highly potent, orally bioavailable, may be brain penetrant, and have higher effectiveness at lower doses than tacrine and acetazolamide. After detailed investigations both in vitro and in silico, novel N -substituted sulfonyl amide derivatives ( 6a–j ) were determined to be highly potent inhibitors for AChE and h CAs ( K I s are in the range of 23.11–52.49 nM, 18.66–59.62 nM, and 9.33–120.80 nM for AChE, h CA I, and h CA II, respectively). Moreover, according to the cytotoxic effect studies, such as the ADME-Tox, cortex neuron cells, and neuroblastoma SH-SY5Y cell line, compounds 6a , 6d , and 6h , which are the most potent representative versus the target enzymes, were identified as orally bioavailable, highly selective, and brain preferentially distributed AChEIs and h CAIs. The docking studies revealed precise binding modes between 6a , 6d , and 6h and h CA II, h CA I, and AChE, respectively. The results presented here might provide a solid basis for further investigation into more potent AChEIs and h CAIs. Graphical abstract The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and hCAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and antiobesity antiepileptic, anticancer, antiinfective, antiglaucoma, and diuretic effects. Here, it has been attempted to discover novel multi-target AChEIs and hCAIs that are highly potent, orally bioavailable, may be brain penetrant, and have higher effectiveness at lower doses than tacrine and acetazolamide. After detailed investigations both in vitro and in silico, novel N-substituted sulfonyl amide derivatives (6a-j) were determined to be highly potent inhibitors for AChE and hCAs (K s are in the range of 23.11-52.49 nM, 18.66-59.62 nM, and 9.33-120.80 nM for AChE, hCA I, and hCA II, respectively). Moreover, according to the cytotoxic effect studies, such as the ADME-Tox, cortex neuron cells, and neuroblastoma SH-SY5Y cell line, compounds 6a, 6d, and 6h, which are the most potent representative versus the target enzymes, were identified as orally bioavailable, highly selective, and brain preferentially distributed AChEIs and hCAIs. The docking studies revealed precise binding modes between 6a, 6d, and 6h and hCA II, hCA I, and AChE, respectively. The results presented here might provide a solid basis for further investigation into more potent AChEIs and hCAIs. |
Author | Arslan, Mustafa Güleç, Özcan Demir, Yeliz Beydemir, Şükrü Türkeş, Cüneyt Yeni, Yeşim Ereminsoy, Ergün Hacımüftüoğlu, Ahmet Küfrevioğlu, Ömer İrfan |
Author_xml | – sequence: 1 givenname: Özcan surname: Güleç fullname: Güleç, Özcan organization: Department of Chemistry, Faculty of Arts and Science, Sakarya University – sequence: 2 givenname: Cüneyt orcidid: 0000-0002-2932-2789 surname: Türkeş fullname: Türkeş, Cüneyt email: cuneyt.turkes@erzincan.edu.tr organization: Department of Biochemistry, Faculty of Pharmacy, Erzincan Binali Yıldırım University – sequence: 3 givenname: Mustafa orcidid: 0000-0003-0796-4374 surname: Arslan fullname: Arslan, Mustafa email: marslan@sakarya.edu.tr organization: Department of Chemistry, Faculty of Arts and Science, Sakarya University – sequence: 4 givenname: Yeliz surname: Demir fullname: Demir, Yeliz organization: Department of Pharmacy Services, Nihat Delibalta Göle Vocational High School, Ardahan University – sequence: 5 givenname: Yeşim surname: Yeni fullname: Yeni, Yeşim organization: Department of Medical Pharmacology, Faculty of Medicine, Atatürk University – sequence: 6 givenname: Ahmet surname: Hacımüftüoğlu fullname: Hacımüftüoğlu, Ahmet organization: Department of Medical Pharmacology, Faculty of Medicine, Atatürk University – sequence: 7 givenname: Ergün surname: Ereminsoy fullname: Ereminsoy, Ergün organization: Department of Chemistry, Faculty of Science, Atatürk University – sequence: 8 givenname: Ömer İrfan surname: Küfrevioğlu fullname: Küfrevioğlu, Ömer İrfan organization: Department of Chemistry, Faculty of Science, Atatürk University – sequence: 9 givenname: Şükrü surname: Beydemir fullname: Beydemir, Şükrü organization: Department of Biochemistry, Faculty of Pharmacy, Anadolu University, The Rectorate of Bilecik Şeyh Edebali University |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35397086$$D View this record in MEDLINE/PubMed |
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Keywords | 1,3,4-oxadiazol Carbonic anhydrase Acetylcholinesterase substituted sulfonyl amide In silico study N-substituted sulfonyl amide |
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Snippet | The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and
h
CAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and... The acetylcholinesterase and carbonic anhydrase inhibitors (AChEIs and hCAIs) remain key therapeutic agents for many bioactivities such as anti-Alzheimer and... |
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SubjectTerms | Bioavailability Biochemistry Biomedical and Life Sciences Cytotoxicity Life Sciences Organic Chemistry Original Original Article Pharmacy Polymer Sciences |
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Title | Cytotoxic effect, enzyme inhibition, and in silico studies of some novel N-substituted sulfonyl amides incorporating 1,3,4-oxadiazol structural motif |
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