In vitro acetylcholinesterase inhibitory activities of fractions and iso-agelasine C isolated from the marine sponge Agelas nakamurai

N.A.

Makale detayları

In vitro acetylcholinesterase inhibitory activities of fractions and iso-agelasine C isolated from the marine sponge Agelas nakamurai

Yazarlar:

N.A.

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.26 Issue 2, pp.279-286

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346336

pISSN:

2630-6344

Anahtar kelimeler:

Özet:

 The marine sponges with their unique and wide range of biodiversity, producing unusual metabolites emerge as a good candidate for new therapeutic agents, including as acetylcholinesterase AChE inhibitor. The aims of this study are to evaluate the potency of fractions and isolated compound from Agelas nakamurai as AChE inhibitor, as well as to determine the structure of the isolated compound. The bioassay-guided isolation protocol was carried out in this study. The AChE inhibitory assay was carried out based on the modified Ellmans method. The structure of the isolated compound was determined by NMR spectroscopy and mass spectrometry. A diterpene alkaloid was isolated from the active fraction of A. nakamurai. This compound exhibited a molecular ion at mz 422.3280 M in mass spectrometry. The UV profile of the isolated compound showed a strong peak at 269 nm, and the specific rotation value is α20D 28,0 MeOH, c 0.25. These data together with the 1H and 13C NMR spectroscopy data are similar to that reported for iso-agelasine C. The isolated iso-agelasine C gave moderate inhibition against AChE enzyme with an IC50 value of 30.68  0.92 µgmL, which was lower compared to the extract and fractions. The stronger AChE inhibitory activity in the extract and fractions is possibly due to the synergistic activity of compounds present in the extract and fractions of A. nakamurai. Iso-agelasine C could serve as a lead for the development of diterpene alkaloid as an AChE inhibitor.

 The marine sponges with their unique and wide range of biodiversity, producing unusual metabolites emerge as a good candidate for new therapeutic agents, including as acetylcholinesterase AChE inhibitor. The aims of this study are to evaluate the potency of fractions and isolated compound from Agelas nakamurai as AChE inhibitor, as well as to determine the structure of the isolated compound. The bioassay-guided isolation protocol was carried out in this study. The AChE inhibitory assay was carried out based on the modified Ellmans method. The structure of the isolated compound was determined by NMR spectroscopy and mass spectrometry. A diterpene alkaloid was isolated from the active fraction of A. nakamurai. This compound exhibited a molecular ion at mz 422.3280 M in mass spectrometry. The UV profile of the isolated compound showed a strong peak at 269 nm, and the specific rotation value is α20D 28,0 MeOH, c 0.25. These data together with the 1H and 13C NMR spectroscopy data are similar to that reported for iso-agelasine C. The isolated iso-agelasine C gave moderate inhibition against AChE enzyme with an IC50 value of 30.68  0.92 µgmL, which was lower compared to the extract and fractions. The stronger AChE inhibitory activity in the extract and fractions is possibly due to the synergistic activity of compounds present in the extract and fractions of A. nakamurai. Iso-agelasine C could serve as a lead for the development of diterpene alkaloid as an AChE inhibitor.

 The marine sponges with their unique and wide range of biodiversity, producing unusual metabolites emerge as a good candidate for new therapeutic agents, including as acetylcholinesterase AChE inhibitor. The aims of this study are to evaluate the potency of fractions and isolated compound from Agelas nakamurai as AChE inhibitor, as well as to determine the structure of the isolated compound. The bioassay-guided isolation protocol was carried out in this study. The AChE inhibitory assay was carried out based on the modified Ellmans method. The structure of the isolated compound was determined by NMR spectroscopy and mass spectrometry. A diterpene alkaloid was isolated from the active fraction of A. nakamurai. This compound exhibited a molecular ion at mz 422.3280 M in mass spectrometry. The UV profile of the isolated compound showed a strong peak at 269 nm, and the specific rotation value is α20D 28,0 MeOH, c 0.25. These data together with the 1H and 13C NMR spectroscopy data are similar to that reported for iso-agelasine C. The isolated iso-agelasine C gave moderate inhibition against AChE enzyme with an IC50 value of 30.68  0.92 µgmL, which was lower compared to the extract and fractions. The stronger AChE inhibitory activity in the extract and fractions is possibly due to the synergistic activity of compounds present in the extract and fractions of A. nakamurai. Iso-agelasine C could serve as a lead for the development of diterpene alkaloid as an AChE inhibitor.

 The marine sponges with their unique and wide range of biodiversity, producing unusual metabolites emerge as a good candidate for new therapeutic agents, including as acetylcholinesterase AChE inhibitor. The aims of this study are to evaluate the potency of fractions and isolated compound from Agelas nakamurai as AChE inhibitor, as well as to determine the structure of the isolated compound. The bioassay-guided isolation protocol was carried out in this study. The AChE inhibitory assay was carried out based on the modified Ellmans method. The structure of the isolated compound was determined by NMR spectroscopy and mass spectrometry. A diterpene alkaloid was isolated from the active fraction of A. nakamurai. This compound exhibited a molecular ion at mz 422.3280 M in mass spectrometry. The UV profile of the isolated compound showed a strong peak at 269 nm, and the specific rotation value is α20D 28,0 MeOH, c 0.25. These data together with the 1H and 13C NMR spectroscopy data are similar to that reported for iso-agelasine C. The isolated iso-agelasine C gave moderate inhibition against AChE enzyme with an IC50 value of 30.68  0.92 µgmL, which was lower compared to the extract and fractions. The stronger AChE inhibitory activity in the extract and fractions is possibly due to the synergistic activity of compounds present in the extract and fractions of A. nakamurai. Iso-agelasine C could serve as a lead for the development of diterpene alkaloid as an AChE inhibitor.

Makale detayları

In vitro acetylcholinesterase inhibitory activities of fractions and iso-agelasine C isolated from the marine sponge Agelas nakamurai

Yazarlar:

N.A.

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.26 Issue 2, pp.279-286

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346336

pISSN:

2630-6344

Alzheimer’s diseas

acetylcholinesterase inhibitor

marine sponge

Agelas nakamurai

iso-agelasine C

Sayı

Makale detayları

In vitro acetylcholinesterase inhibitory activities of fractions and iso-agelasine C isolated from the marine sponge Agelas nakamurai

Yazarlar: N.A.

Yayıncı: Marmara University

Ana Başlıklar: Pharmaceutical Sciences

Dergi: Journal of Research in Pharmacy Vol.26 Issue 2, pp.279-286

Belge Tipi: Makale

Yayın Tarihi: 6/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001346336

pISSN: 2630-6344

Alzheimer’s diseas

acetylcholinesterase inhibitor

marine sponge

Agelas nakamurai

iso-agelasine C

Sayı

Yazarlar:

N.A.

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.26 Issue 2, pp.279-286

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346336

pISSN:

2630-6344