Article Per Year (5 Year)
p-Index From 2021 - 2026
0.444
P-Index
This Author published in this journals
All Journal Narra J
Cuandra, Kevin N.
Unknown Affiliation
Biochemistry, Genetics & Molecular Biology Health Professions Immunology & microbiology Medicine & Pharmacology Public Health

Published : 2 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 2 Documents
Search

 1 
Unraveling the power of peptides from Cucumaria frondosa coelomic fluid as multitarget therapy of diabetic kidney disease: An in-silico study Rita, Rauza S.; Cuandra, Kevin N.; Nasri, Syahidatul A.; Carmenita, Mutiara A.; Kristaningtyas, Nathania A.; Rasendriya, Daffa Z.; Maulana, Rafi; Hibatullah, Muhammad N.; Yahono, Angela S.; Afdhal, Fitrah; Ibrahim, Filzatuz Z.; Nayu, Balqist K.; Teguh, Muhammad
Narra J Vol. 5 No. 1 (2025): April 2025
Publisher : Narra Sains Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.52225/narra.v5i1.1180

Abstract

Diabetic kidney disease is a condition characterized by persistent albuminuria, diabetic glomerular lesions, and a reduced glomerular filtration rate in people with diabetes. Peptides in Cucumaria frondosa coelomic fluid have been proven to provide antidiabetic and anti-inflammatory activity that can be used as one of the innovations in developing a multitarget therapy, especially in diabetic kidney disease. Therefore, the aim of this study was to unravel the power of peptide-based metabolites from C. frondosa coelomic fluid as multitarget therapy for diabetic kidney disease using an in-silico study. UCSF Chimera software was utilized to construct the three-dimensional structure of coelomic fluid peptides from C. frondosa. The toxicity and allergenicity of peptides were examined using the ToxinPred and AllerTop websites, respectively. From the PDBJ database, the 3D structures of protein kinase B, alpha isoform (AKT1); vascular endothelial growth factor receptor 2 (VEGFR2); epidermal growth factor receptor (EGFR); α-glucosidase; and glucokinase were obtained. Molecular docking was carried out using MOE Software. In this in-silico study, peptide 9 (-10.32 kcal/mol), peptide 1 (-9.41 kcal/mol), and peptide 3 (-9.55 kcal/mol) were shown to act as specific adenosine triphosphate-competitive inhibitors of EGFR, AKT1, and VEGFR2, respectively. Peptide 8 (-11.06 kcal/mol) can specifically inhibit α-glucosidase by binding to its active site. Peptide 1 (-9.80 kcal/mol) is predicted to specifically inhibit glucokinase activity by blocking its active side. Molecular dynamics simulations confirmed stable interactions with receptor proteins. In conclusion, C. frondosa coelomic fluid peptides have been shown not only to alleviate diabetic kidney disease but also to stabilize blood glucose levels and prevent hyperglycemia based on in-silico analysis.
In silico analysis of Arbacia lixula-derived peptides and plasmid construction for recombinant anti-aging therapies Yenny, Satya W.; Jamsari, Jamsari; Hazmi, Auliya A.; Cuandra, Kevin N.; Hanifah, Wafiq; Yahono, Angela S.; Wahyudi, Dhyani P.; Buana, Gherriandi R.; Rahman, Awalil RK.; Maharani, Annisa D.; Firjatullah, Muhammad F.; Maulana, Rafi; Prayogi, Norbertus M.; Tristan, Christopher D.
Narra J Vol. 4 No. 3 (2024): December 2024
Publisher : Narra Sains Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.52225/narra.v4i3.1283

Abstract

Skin aging is one of the degenerative processes influenced by tyrosinase, elastase, collagenase, hyaluronidase, and matrix metalloproteinase-9 (MMP9) activity. One promising avenue for discovering antiaging therapeutics is the peptides from the Arbacia lixula spine. The aim of this study was to explore the potential of peptides from A. lixula spine as a multitarget inhibitor for recombinant antiaging therapies through in silico approaches. The crystal structure of peptides previously identified in A. lixula spine was visualized using the UCSF Chimera. The protein data bank (PDB) database was used to obtain the crystal structures of protein targets. The webservers Innovagen, AllerTop, and ToxinPred were utilized to predict the peptide's water solubility, toxicity, and allergenicity. MOE application was used to prepare all ligands and proteins, molecular docking, and visualization. Molecular dynamics simulations were carried out on the protein-ligand complexes on Yasara Dynamics application. The Benchling website was used to perform virtual electrophoresis and reconstruct the recombinant plasmid (Psb1c3). Based on the molecular docking results, peptide REGSPDLLE has the potential as a multitarget inhibitor of tyrosinase (-9.07 kcal/mol), hyaluronidase (-10.57 kcal/mol), elastase (-9.32 kcal/mol), collagenase (-10.57 kcal/mol), and MMP9 (-10.43 kcal/mol). Peptide REGSPDLLE was selected due to its strong binding affinity on the active site of each target protein and exhibits non-toxic, non-allergenic, and good water-soluble as indicated by Support Vector Machine score <0. Molecular dynamics simulations confirmed stable interactions with receptor proteins. Peptide REGSPDLLE was successfully inserted into the recombinant pSB1C3 plasmid, confirmed by virtual electrophoresis with bands at ~2000 bp and ~150 bp. Further in vitro and in vivo studies are necessary to verify the anti-aging efficacy of peptide REGSPDLLE.
Co-Authors Afdhal, Fitrah Buana, Gherriandi R. Carmenita, Mutiara A. Firjatullah, Muhammad F. Hanifah, Wafiq Hazmi, Auliya A. Hibatullah, Muhammad N. Ibrahim, Filzatuz Z. Jamsari Jamsari Kristaningtyas, Nathania A. Maharani, Annisa D. Maulana, Rafi MUHAMMAD TEGUH, MUHAMMAD Nasri, Syahidatul A. Nayu, Balqist K. Prayogi, Norbertus M. Rahman, Awalil RK. Rasendriya, Daffa Z. Rita, Rauza S. Tristan, Christopher D. Wahyudi, Dhyani P. Yahono, Angela S. Yenny, Satya W.