Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies

Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosid...
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Autor*in:	Ogunyemi, O. M. [verfasserIn] Gyebi, A. G. [verfasserIn] Adebayo, J. O. [verfasserIn] Oguntola, J. A. [verfasserIn] Olaiya, C. O. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	Pregnanes Pregnane glycosides Nutraceuticals Diabetes In silico

Übergeordnetes Werk:	Enthalten in: SN applied sciences - [Cham] : Springer International Publishing, 2019, 2(2020), 12 vom: 01. Dez.
Übergeordnetes Werk:	volume:2 ; year:2020 ; number:12 ; day:01 ; month:12

Links:	Volltext

DOI / URN:	10.1007/s42452-020-03951-0

Katalog-ID:	SPR042217695

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245	1	0	\|a Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
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520			\|a Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb.
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700	1		\|a Adebayo, J. O. \|e verfasserin \|4 aut
700	1		\|a Oguntola, J. A. \|e verfasserin \|4 aut
700	1		\|a Olaiya, C. O. \|e verfasserin \|4 aut
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912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_138
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2107
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
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Indexfelder

author_variant	o m o om omo a g g ag agg j o a jo joa j a o ja jao c o o co coo
matchkey_str	article:25233971:2020----::ascoeoadtepennpyohmcldrvdrmogoeaaioimsmlsadlcsdsihbt
hierarchy_sort_str	2020
bklnumber	50.00 35.00 33.00
publishDate	2020
allfields	10.1007/s42452-020-03951-0 doi (DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e DE-627 ger DE-627 rakwb eng 500 ASE 500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Ogunyemi, O. M. verfasserin aut Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb. Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213 Gyebi, A. G. verfasserin aut Adebayo, J. O. verfasserin aut Oguntola, J. A. verfasserin aut Olaiya, C. O. verfasserin aut Enthalten in SN applied sciences [Cham] : Springer International Publishing, 2019 2(2020), 12 vom: 01. Dez. (DE-627)103761139X (DE-600)2947292-1 2523-3971 nnns volume:2 year:2020 number:12 day:01 month:12 https://dx.doi.org/10.1007/s42452-020-03951-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 50.00 ASE 35.00 ASE 33.00 ASE AR 2 2020 12 01 12
spelling	10.1007/s42452-020-03951-0 doi (DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e DE-627 ger DE-627 rakwb eng 500 ASE 500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Ogunyemi, O. M. verfasserin aut Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb. Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213 Gyebi, A. G. verfasserin aut Adebayo, J. O. verfasserin aut Oguntola, J. A. verfasserin aut Olaiya, C. O. verfasserin aut Enthalten in SN applied sciences [Cham] : Springer International Publishing, 2019 2(2020), 12 vom: 01. Dez. (DE-627)103761139X (DE-600)2947292-1 2523-3971 nnns volume:2 year:2020 number:12 day:01 month:12 https://dx.doi.org/10.1007/s42452-020-03951-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 50.00 ASE 35.00 ASE 33.00 ASE AR 2 2020 12 01 12
allfields_unstemmed	10.1007/s42452-020-03951-0 doi (DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e DE-627 ger DE-627 rakwb eng 500 ASE 500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Ogunyemi, O. M. verfasserin aut Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb. Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213 Gyebi, A. G. verfasserin aut Adebayo, J. O. verfasserin aut Oguntola, J. A. verfasserin aut Olaiya, C. O. verfasserin aut Enthalten in SN applied sciences [Cham] : Springer International Publishing, 2019 2(2020), 12 vom: 01. Dez. (DE-627)103761139X (DE-600)2947292-1 2523-3971 nnns volume:2 year:2020 number:12 day:01 month:12 https://dx.doi.org/10.1007/s42452-020-03951-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 50.00 ASE 35.00 ASE 33.00 ASE AR 2 2020 12 01 12
allfieldsGer	10.1007/s42452-020-03951-0 doi (DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e DE-627 ger DE-627 rakwb eng 500 ASE 500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Ogunyemi, O. M. verfasserin aut Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb. Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213 Gyebi, A. G. verfasserin aut Adebayo, J. O. verfasserin aut Oguntola, J. A. verfasserin aut Olaiya, C. O. verfasserin aut Enthalten in SN applied sciences [Cham] : Springer International Publishing, 2019 2(2020), 12 vom: 01. Dez. (DE-627)103761139X (DE-600)2947292-1 2523-3971 nnns volume:2 year:2020 number:12 day:01 month:12 https://dx.doi.org/10.1007/s42452-020-03951-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 50.00 ASE 35.00 ASE 33.00 ASE AR 2 2020 12 01 12
allfieldsSound	10.1007/s42452-020-03951-0 doi (DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e DE-627 ger DE-627 rakwb eng 500 ASE 500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Ogunyemi, O. M. verfasserin aut Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb. Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213 Gyebi, A. G. verfasserin aut Adebayo, J. O. verfasserin aut Oguntola, J. A. verfasserin aut Olaiya, C. O. verfasserin aut Enthalten in SN applied sciences [Cham] : Springer International Publishing, 2019 2(2020), 12 vom: 01. Dez. (DE-627)103761139X (DE-600)2947292-1 2523-3971 nnns volume:2 year:2020 number:12 day:01 month:12 https://dx.doi.org/10.1007/s42452-020-03951-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 50.00 ASE 35.00 ASE 33.00 ASE AR 2 2020 12 01 12
language	English
source	Enthalten in SN applied sciences 2(2020), 12 vom: 01. Dez. volume:2 year:2020 number:12 day:01 month:12
sourceStr	Enthalten in SN applied sciences 2(2020), 12 vom: 01. Dez. volume:2 year:2020 number:12 day:01 month:12
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Pregnanes Pregnane glycosides Nutraceuticals Diabetes In silico
dewey-raw	500
isfreeaccess_bool	false
container_title	SN applied sciences
authorswithroles_txt_mv	Ogunyemi, O. M. @@aut@@ Gyebi, A. G. @@aut@@ Adebayo, J. O. @@aut@@ Oguntola, J. A. @@aut@@ Olaiya, C. O. @@aut@@
publishDateDaySort_date	2020-12-01T00:00:00Z
hierarchy_top_id	103761139X
dewey-sort	3500
id	SPR042217695
language_de	englisch
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author	Ogunyemi, O. M.
spellingShingle	Ogunyemi, O. M. ddc 500 bkl 50.00 bkl 35.00 bkl 33.00 misc Pregnanes misc Pregnane glycosides misc Nutraceuticals misc Diabetes misc In silico Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
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topic_title	500 ASE 50.00 bkl 35.00 bkl 33.00 bkl Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies Pregnanes (dpeaa)DE-He213 Pregnane glycosides (dpeaa)DE-He213 Nutraceuticals (dpeaa)DE-He213 Diabetes (dpeaa)DE-He213 In silico (dpeaa)DE-He213
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title	Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
ctrlnum	(DE-627)SPR042217695 (DE-599)SPRs42452-020-03951-0-e (SPR)s42452-020-03951-0-e
title_full	Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
author_sort	Ogunyemi, O. M.
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author_browse	Ogunyemi, O. M. Gyebi, A. G. Adebayo, J. O. Oguntola, J. A. Olaiya, C. O.
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title_sort	marsectohexol and other pregnane phytochemicals derived from gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
title_auth	Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
abstract	Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb.
abstractGer	Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb.
abstract_unstemmed	Abstract This study employed in vitro and in silico techniques to screen isolated pregnane phytochemicals (P1–P4), as well as their source pregnane-rich chromatographic fractions, which were derived from Gongronema latifolium Benth (GLB), for their inhibitory potentials against α-amylase, α-glucosidase, and sucrase enzyme activities. The results show that, most pregnane-rich chromatographic fractions and isolated compounds exhibited good inhibitory activities against α-amylase, and α-glucosidase enzymes. Among the isolated compounds, marsectohexol (P2) is the most favourable structure that showed inhibition against α-amylase ($ IC_{50} $ = 3.712 µg/mL) when compared with the reference inhibitor, acarbose (($ IC_{50} $ = 15.418 µg/mL). Based on negative and low value of ∆G (Gibb’s free energy), docking scores revealed that, marsectohexol has the highest binding affinity (− 8.8 kcal/mol) to human pancreatic α-amylase (HPA) as compared to the standard acarbose (− 8.1 kcal/mol). Marsectohexol and the other phytocompounds were also found to dock into the active site of HPA; interacting with key catalytic amino acid residues (ASP197, GLU233 and ASP300), which are known to involve in the nucleophilic, and the acid/base catalysis of the enzyme. Although, the pregnane phytocompounds have considerable high affinity binding to the human lysosomal α-glucosidase, they interacted with pockets other than the active site. In conclusion, at least, marsectohexol and three other constituent pregnane phytochemicals of GLB are potential inhibitors of the carbohydrate-hydrolyzing enzymes. These compounds may account for the anti-hyperglyceamic and antidiabetic potentials of this food herb.
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container_issue	12
title_short	Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies
url	https://dx.doi.org/10.1007/s42452-020-03951-0
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author2	Gyebi, A. G. Adebayo, J. O. Oguntola, J. A. Olaiya, C. O.
author2Str	Gyebi, A. G. Adebayo, J. O. Oguntola, J. A. Olaiya, C. O.
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doi_str	10.1007/s42452-020-03951-0
up_date	2024-07-04T01:18:48.007Z
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Marsectohexol and other pregnane phytochemicals derived from Gongronema latifolium as α-amylase and α-glucosidase inhibitors: in vitro and molecular docking studies

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