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Review
. 2023 Apr 28;21(5):283.
doi: 10.3390/md21050283.

A Bibliometric and In Silico-Based Analysis of Anti-Lung Cancer Compounds from Sea Cucumber

Afshin Zare  1 , Safoura Izanloo  2   3 , Sajed Khaledi  4 , Mussin Nadiar Maratovich  5 , Asset Askerovich Kaliyev  5 , Nurgul Abdullayevna Abenova  6 , Farhad Rahmanifar  7 , Mahdi Mahdipour  8   9 , Shabnam Bakhshalizadeh  10   11 , Reza Shirazi  12 , Nader Tanideh  1   13   14 , Amin Tamadon  1   15
Affiliations
Review

A Bibliometric and In Silico-Based Analysis of Anti-Lung Cancer Compounds from Sea Cucumber

Afshin Zare et al. Mar Drugs. .

Abstract

Lung cancer is one of the most lethal malignancies in the world. However, current curative approaches for treating this type of cancer have some weaknesses. Therefore, scientists are attempting to discover new anti-lung cancer agents. Sea cucumber is a marine-derived source for discovering biologically active compounds with anti-lung cancer properties. To explore the anti-lung cancer properties of sea cucumber, we analyzed surveys using VOSviewer software and identified the most frequently used keywords. We then searched the Google Scholar database for compounds with anti-lung cancer properties within that keyword family. Finally, we used AutoDock 4 to identify the compounds with the highest affinity for apoptotic receptors in lung cancer cells. The results showed that triterpene glucosides were the most frequently identified compounds in studies examining the anti-cancer properties of sea cucumbers. Intercedenside C, Scabraside A, and Scabraside B were the three triterpene glycosides with the highest affinity for apoptotic receptors in lung cancer cells. To the best of our knowledge, this is the first time that anti-lung cancer properties of sea cucumber-derived compounds have been examined in in silico conditions. Ultimately, these three components displayed anti-lung cancer properties in in silico conditions and may be used for the manufacture of anti-lung cancer agents in the near future.

Keywords: anti-cancer agents; apoptosis; bibliometrics; glucosides; in silico techniques; lung neoplasms; marine biology; sea cucumbers; triterpenes.

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Conflict of interest statement

The authors Afshin Zare, Amin Tamadon, and Nader Tanideh were employed by PerciaVista R&D Co. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
The number of studies examining the anti-cancer effects of sea cucumber from 1973 to 2023.
Figure 2
Figure 2
The most frequent keywords in the surveys that have studied the anti-cancer features of sea cucumber. The size of each keyword represents the frequency of it.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 3
Figure 3
The molecules and interactions that are involved in the binding site of best binding conformation between Intercedenside C, Scabraside A, and Scabraside B and the apoptotic receptors in lung cancer cells. The interactions between Intercedenside C and following receptors: Fas R. (A), Tumor necrosis factor receptor 1 (TNFR1) (B), Death receptor 4 (DR4) (C), Death receptor 5 (DR5) (D), Peroxisome proliferator-activated receptor gamma (PPAR-γ) (F), Caspase-3 (G), Caspase-8 (I), Cannabinoid receptor type 1 (CB1) (K), Cannabinoid receptor type 2 (CB2) (L), Toll-like receptor 4 (TLR- 4) (M), Toll-like receptor 9 (TLR- 9) (N), Metabotropic glutamate receptor 8 (mGluR 8) (P), Prostaglandin D2 (PGD2) (Q), Transforming Growth Factor Beta Receptor 2 (TGFBR2) (R), Scabraside A with Caspase-9 (J), and Scabraside B with the three following receptors: Insulin-like growth factor 1 (IGF-1) (E), Caspase-7 (H), and Endothelial protein C receptor (EPCR) (O) are demonstrated in detail.
Figure 4
Figure 4
The 2D structure of Intercedenside C and Scabrasides A and B.
Figure 5
Figure 5
The role of the Fas receptor in the process of apoptosis in lung cancer cells.
Figure 6
Figure 6
The role of the TNFR1 receptor in the process of apoptosis in lung cancer cells.
Figure 7
Figure 7
The role of the DR4 and DR5 receptors in the process of apoptosis in lung cancer cells.
Figure 8
Figure 8
The role of the PPAR-γ receptor in the process of apoptosis in lung cancer cells.
Figure 9
Figure 9
The role of CB1 and CB2 receptor in the process of apoptosis in lung cancer cells.
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