Article Per Year (5 Year)
p-Index From 2021 - 2026
2.668
P-Index
This Author published in this journals
All Journal INDONESIAN JOURNAL OF LEGAL AND FORENSIC SCIENCES Jurnal Kimia (Journal of Chemistry) Buletin Udayana Mengabdi Jurnal Farmasi Udayana Indonesian Journal of Cancer Chemoprevention Indonesian Journal of Pharmaceutical Science and Technology INDONESIAN JOURNAL OF PHARMACY JPSCR : Journal of Pharmaceutical Science and Clinical Research Journal of Health Sciences and Medicine Jurnal Ilmiah Medicamento Pharmacy Reports Prosiding Workshop dan Seminar Nasional Farmasi (WSNF)
Ni Putu Linda Laksmiani
Jurusan Farmasi Fakultas Matematika Dan Ilmu Pengetahuan Alam Universitas Udayana
Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Dentistry Education Environmental Science Health Professions Immunology & microbiology Law, Crime, Criminology & Criminal Justice Materials Science & Nanotechnology Medicine & Pharmacology Public Health

Published : 57 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 57 Documents
Search

 2   3   4   5   6 
The potency of alpha-humulene as HER-2 inhibitor by molecular docking Putra, I Made Harimbawa; Pratama, I Putu Ari Anggara Catur; Putra, Komang Dian Aditya; Pradnyaswari, G. A. Desya; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 2 No. 1 (2022): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (813.372 KB) | DOI: 10.51511/pr.19

Abstract

HER-2 overexpression is present in approximately 20% of breast cancer. This research aims to study the interactions of α-humulene to HER-2 protein by using in silico molecular docking. The experiment was carried out by HER-2 protein preparation (PDB ID 3PP0), docking validation, α-humulene optimization, and α-humulene docking. The results showed that α-humulene had binding energy of -7.50 kcal/mol, Van der Waals binding energy of -7.48 kcal/mol, and electrostatic energy of -0.02 kcal/mol. α-Humulene is potential as anti-breast cancer towards HER-2 in silico.
The potency of blumeatin and luteolin as caspase-1 inhibitor by molecular docking Pratama, I Putu Ari Anggara Catur; Putra, I Made Harimbawa; Pujasari, Luh Wayan Sita; Dewi, Komang Dian Merta Sari; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 2 No. 1 (2022): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (588.097 KB) | DOI: 10.51511/pr.22

Abstract

COVID-19 infection induces inflammation by increasing cytokines such as IL-1b, IL-6, IL-18, IFN-γ, and TNF-α. IL-1b is generated by the involvement of caspase-1. Therefore, caspase-1 inhibitor can be potential for inflammation therapy caused by COVID-19 infection. This study aims to determine the potential of blumeatin and luteolin as anti-inflammatory agents by inhibiting caspase-1 using a molecular docking approach. This study was carried out by caspase-1 (PDB ID: 1RWK) preparation, blumeatin and luteolin structure optimization, docking protocol validation, and docking of blumeatin and luteolin on caspase-1. Bluematin and luteolin had a binding affinity of -5,63 kcal/mol and -5,93 kcal/mol, lower than Q158 native ligand (-3.92 kcal/mol). Similar amino acid residues in hydrogen bonds interaction were observed between Q158 native ligand, blumeatin, and luteolin with caspase-1 (GLN 283 and ARG 179). Blumeatin and luteolin are potentially anti-inflammation agents through the inhibition of the caspase-1 in silico.
Exploring the binding affinity of rutin, catechin, and epicatechin to ALK and caspase-3: implications for colorectal cancer treatment Adhyaksa, I Nyoman Mahesa Praba; Pramesti, Ni Luh Putu Cintya; Susanti, Ni Made Pitri; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 2 No. 2 (2022): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.51511/pr.56

Abstract

This study explores the interaction of rutin, catechins, and epicatechins with anaplastic lymphoma kinase (ALK) and caspase-3, focusing on their potential role in modulating the apoptotic mechanisms in colorectal cancer cells. The experimental approach included the preparation of ALK (PDB ID: 5USQ) and caspase-3 (PDB ID: 2XZT), validation of the docking process, optimization of the test compounds, and docking analyses. The molecular docking methodology was validated with an RMSD value of ≤ 3 Å. The docking outcomes revealed that rutin, catechins, and epicatechin exhibited lower binding affinity to ALK, with binding energies of -8.58 kcal/mol, -8.41 kcal/mol, and -7.82 kcal/mol, respectively, compared to ALK's native ligand (-10.27 kcal/mol). Conversely, these compounds demonstrated higher affinity to caspase-3 than its native ligand (-2.54 kcal/mol), with binding energies of -6.03 kcal/mol for rutin, -5.28 kcal/mol for catechins, and -4.95 kcal/mol for epicatechin. These findings suggest that rutin, catechins, and epicatechins hold promise as colorectal anticancer agents by potentially modulating the activity of ALK and caspase-3 through inhibition and activation mechanisms, respectively.
The potency of pinostrobin and pinocembrin as antiphotoaging agents: in silico study Pradnyana, I Gusti Ngurah Agung; Putri, Ketut Yuantarisa Kartika; Susanti, Ni Made Pitri; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 2 No. 2 (2022): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.51511/pr.58

Abstract

Photoaging occurs when the skin ages due to ultraviolet light exposure. Phenolic compounds generally possess antioxidant activity, which helps prevent the formation of free radicals caused by sunlight exposure. This study explores the potential of pinostrobin and pinocembrin as antiphotoaging agents through molecular docking against matrix metalloproteinases (MMPs): MMP-1, MMP-3, and MMP-9. We utilized Hyperchem 8 to prepare and optimize the test compound and Chimera 1.11.1 for protein preparation. Validation and docking procedures were conducted using the AutoDockTools 1.5.6 application, with validation confirming that the method was valid with an RMSD value ≤ 3 Å. Both pinostrobin and pinocembrin exhibited an affinity for the target protein, although their affinity was slightly less than that of the native ligand and retinol. In conclusion, pinostrobin and pinocembrin demonstrate an affinity for MMP-1, MMP-3, and MMP-9, indicating their potential as anti-photoaging agents by obstructing the mechanisms of MMP-1, MMP-3, and MMP-9.
Comparative in-silico analysis of vitexin and orientin as potential antiphotoaging agents against MMP enzymes Nyunda, Ricky Putra Banyim; Wiantini, Ni Made Rita; Susanti, Ni Made Pitri; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 3 No. 2 (2023): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.51511/pr.60

Abstract

Photoaging, a result of excessive UV exposure, increases ROS production and collagen degradation by MMPs, causing skin wrinkles and roughness. This study explores the potential of vitexin and orientin as natural antiphotoaging agents through in-silico molecular docking, comparing their efficacy against retinol in inhibiting MMP-1, MMP-3, and MMP-9 enzymes involved in photoaging. The research utilized Hyperchem 8 for compound optimization, Chimera 1.11 for target protein preparation, and AutodockTools 1.5.6 for docking analysis. Results demonstrated that vitexin and orientin exhibit stronger affinity towards MMP-1, MMP-3, and MMP-9, indicated by more negative binding energies than retinol. Their interaction with the MMP enzymes, characterized by specific hydrogen bonds with key amino acid residues, suggests a potent inhibitory effect. This affinity indicates vitexin and orientin’s potential as effective antiphotoaging agents, providing a basis for further exploration in skin care applications.
In silico molecular docking of luteolin as a potential antihyperpigmentation agent Putri, Lucienne Agatha Larasati Nugraha; Anjani, Ni Luh Ari Krisma; Laksmiani, Ni Putu Linda; Susanti, Ni Made Pitri
Pharmacy Reports Vol. 3 No. 1 (2023): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.51511/pr.61

Abstract

Excessive melanin synthesis, often triggered by overexposure to UV rays, is catalyzed by melanogenesis enzymes such as tyrosinase, tyrosinase-related protein 1, and D-dopachrome tautomerase. Derived from natural sources, the flavonoid compound luteolin is explored for its antihyperpigmentation potential. This study assesses luteolin’s efficacy as an antihyperpigmentation agent by analyzing its affinity and bond interactions with melanogenesis enzymes through an in silico approach. Molecular docking, facilitated by HyperChem 8 for test compound optimization and Chimera 1.11.1 for protein preparation, alongside method validation and docking with AutoDockTools 1.5.6, established the protocol’s validity with an RMSD value of ≤3 Å. Docking results reveal luteolin's higher affinity for the target proteins compared to native ligands, with binding energies of -5.63 kcal/mol for tyrosinase, -6.18 kcal/mol for tyrosinase-related protein 1, and -6.54 kcal/mol for D-dopachrome tautomerase. The interaction between luteolin and these proteins involves hydrogen, hydrophobic, electrostatic, and Van der Waals bonds, with amino acid residues His61, Lys129, Arg132 (tyrosinase); His192, His224, Val89 (tyrosinase-related protein 1); and Ile64, Asn73 (D-dopachrome tautomerase) participating in hydrogen bond formation. These findings suggest luteolin’s significant potential as an antihyperpigmentation agent by inhibiting melanogenesis enzymes.
Exploring the anticancer potential of scopoletin against HER-2 positive breast cancer: an in silico molecular docking study Adhyaksa, I Nyoman Mahesa Praba; Silawarti, Putu Ayu Karunia; Putra, Made Ferdio Amarta; Laksmiani, Ni Putu Linda
Pharmacy Reports Vol. 3 No. 2 (2023): Pharmacy Reports
Publisher : Indonesian Young Scientist Group and UPN Veteran Jakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.51511/pr.63

Abstract

Cancer, defined by the unchecked growth and invasive potential of abnormal cells, remains a global health challenge. Within this context, scopoletin, a compound isolated from the leaves of Impatiens balsamina L., has garnered attention for its potential as an anti-breast cancer agent. This study employed in silico molecular docking techniques to explore scopoletin's interaction with the HER-2 protein, a known target in breast cancer therapy. The docking analysis revealed that scopoletin exhibits affinity towards the HER-2 protein, with a binding energy of -6.3 kcal/mol. Notably, the binding energy of scopoletin is comparable to that of gefitinib, an established cancer drug, further underscoring its potential therapeutic value.
Co-Authors A. A.W. Lestari A. B. S. Pawarrangan A.A. Bagus Yoga Saputra A.A.I.K. Dewi Adhyaksa, I Nyoman Mahesa Praba Adiluhur M. A. Anak Agung Intan Kharisma Dewi Andika Prayoga Andini, Kadek Lia Anggreni, Ni Ketut Sri Anggreni, Ni Putu Ruscita Anjani, Ni Luh Ari Krisma Arifin, Muhammad Fajar Arimbawa I.B.S. Cahyani, Ni Ketut Nitya Cokorda Istri Sri Arisanti Cokorda Istri Tirta Rusmala Dewi Coky N. W. C. D.M. Nita Pratiwi Deddi Prima Putra Dewa Ayu Pramesti Utari Dewa Ayu Swastini Dewantari A. A. I. S. H Dewi L. R. Dewi Puspita Apsari Dewi, Cokorda Istri Tirta Rusmala Dewi, Komang Dian Merta Sari Dewi, Ni Kadek Diah Parwati Diarini A. S. Dwivayana, I Kadek Diva E.I. Setyawan Edy Meiyanto Febyani, Putu Dewi Fitriari, Diah Mawarni G. A. K. Amarawati G.A.D. Mayagita H. Prabowo I G.P. Putra I Gusti Ayu Made Srinadi I Gusti Ngurah Agung Dewantara Putra I K. Duantara I K. N. Sanjaya I K.N. Sanjaya I Ketut Gede Gilang Gama Harta I Komang Niko Sanjaya I Made Agus Gelgel Wirasuta I N.K. Widjaja I Nengah Kadjeng Widjaja I P.W. I P. W. Nugraha I P.Y. Astara Putra I W. A. Widiantara I W. I. Prayoga I W. Suwartawan I.G.A. Januarta I.G.N.A.D. Putra I.K. Subagia I.N.K. Widjaja I.P. Priyasana Ida Bagus Gde Agung Raditya Eka Putra K. D. Adnyani K. D. Adnyani K. M. Arianti K. R. Reynaldi K.M. Limba K.R Suciptha K.W. Astuti Kadek Joni Prayoga Ketut Widyani Astuti Ketut Yuantarisa Kartika Putri Krisnayana, I Gede Bayu L. W. E. Lestari L.P.F. Larasanty M. A. P. P. Rashid M. B. O. Rastini M. D. Widyastuti M. I. Widiastari Mahaswari, Anak Agung Istri Rani Mirayanti, Ni Putu Dinda N. K. M. Giantari N. K. M. Giantari N. K. M. Noviyanti N. K.S. Ani N. L. P. V. Paramita N.K. Cornelia Ayu Trisna N.N.A.S. Devi N.P.A.D. Wijayanti N.P.M.P.P. Winarni N.PA.D. Wijayanti Ni Kadek Warditiani Ni Luh Ari Krisma Anjani Ni Luh Putu Cintya Pramesti Ni Made Ary Sarasmita Ni Made Pitri Susanti Ni Made Rita Wiantini Ni Putu Ayu Dewi Wijayanti Ni Putu Diah Kusuma Dewi Ni Putu Eka Leliqia Ni Putu Eka Sulastini Ni Putu Ruscita Anggreni Ni Wayan Intan Indayanti Nyunda, Ricky Putra Banyim Oka M. P. A. I. A. Siaka P. V. P. Putri P.D. Wilantari P.P. Pramita Dewi Pande Made Nova Armita Sari, Pande Made Nova Pradnyana Putra Pradnyana, I Gusti Ngurah Agung Pradnyaswari, G. A. Desya Pramesti, Ni Luh Putu Cintya Pratama, I Putu Ari Anggara Catur Pujasari, Luh Wayan Sita Purnama, I.G.P.P Putra, I Made Harimbawa Putra, Komang Dian Aditya Putra, Made Ferdio Amarta Putri, Ketut Yuantarisa Kartika Putri, Lucienne Agatha Larasati Nugraha Putri, Putu Rika Jesika Putri, Wahyu Nadi Eka Putu Rika Jesika Putri Rashid, M.A.P.P Ratna Asmah Susidarti Rismayanti, A. A. M. I. Ritmaleni, Ritmaleni Rumiyati, Rumiyati Saputra, Made Agus Widiana Sari, Ida Ayu Yadnyaningtias Permata Sasi Ani Silawarti, Putu Ayu Karunia Sismindari . Sonia Sonia Suastika, I.G.A. Sunariyani, P. E. A. Suryadewi, Kadek Dinda Ulfatul Husnaa Utari, Dewa Ayu Pramesti V. Rahmadinha Wayan Suwartawan Wiantini, Ni Made Rita Widjaja, I. N. K. Widjaja, I. N. K.. Winarti, N.W. Wiratama Nugraha Yan Ramona Yudiastra, I.K. Yustiantara, Putu Sanna