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In Vitro α-Glucosidase Enzyme Inhibition Activity Test of Water Extract From Sintok (Cinnamomum sintoc Blume) Bark Saksono, Astrella Amanda Putri; Simanjuntak, Inana Ratu Soripada; Wahjudi, Mariana; Gondokesumo, Marisca Evalina
Pharmaceutical Sciences and Research Vol. 12, No. 1
Publisher : UI Scholars Hub

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Diabetes mellitus is a condition characterized by elevated blood glucose levels beyond the normal limits. One therapeutic approach for managing diabetes mellitus involves inhibiting the α-glucosidase enzyme, which plays a role in glucose absorption in the body. However, the use of oral antidiabetic drugs from the α-glucosidase inhibitor class often causes gastrointestinal side effects. Therefore, exploring natural materials as alternative treatments is a promising option. In Indonesia, one plant with potential as an alternative treatment is sintok (Cinnamomum sintoc Blume), a member of the Cinnamomum genus, which is widely utilized in traditional medicine for chronic diseases such as diabetes mellitus. This study aimed to evaluate the α-glucosidase inhibitory activity of a water extract of sintok bark. Preliminary tests were conducted to determine the optimal conditions for measuring α-glucosidase enzyme inhibition activity in vitro using a UV- vis spectrophotometer. The results showed optimal enzyme activity at a wavelength of 405 nm, an incubation time of 40 minutes, and a substrate concentration of 12.5 mM. The water extract of sintok bark exhibited the highest inhibitory activity at a concentration of 5 ppm, with an inhibition value of 28.66%, while acarbose, used as a positive control, achieved the highest inhibition value of 96.36% at a concentration of 4.5 ppm. In conclusion, the aqueous extract of sintok bark demonstrates inhibitory activity against the α-glucosidase enzyme, indicating its potential as a natural antidiabetic agent.
Pencarian Kandidat Vaksin Tbc Dari Epitope Protein Agj16802.1 (Virulence Factor Mce Family Protein [Mycobacterium Tuberculosis Str. Beijing/Nitr203]) Prasetyaningtyas, Herawati Dwi; Wahjudi, Mariana; Yulanda Antonius
Syntax Literate Jurnal Ilmiah Indonesia
Publisher : Syntax Corporation

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.36418/syntax-literate.v10i9.61696

Abstract

In 2022, the burden of TB in the world was 10,556,328. The incidence of tuberculosis in Indonesia in 2021 was 969,000. The increase in TB incidence in 2021 was 18%. WHO has set a global target and milestone to reduce the incidence of TB by the end of 2030, as well as the Indonesian Ministry of Health. TB can be prevented with the BCG vaccine. BCG avoids phagosome maturation, autophagy, and reduces MHC-II expression of APCs that affect T cell activation by triggering an IgM antibody response, class-switched IgG, to specific proteins ESAT6 and CFP10. Protein subunit vaccines are an option to induce an immune response. Antigens recognized by cells during latent infection and involved in immunological evasion mechanisms or the emergence of CD4+ and CD8+ specific T cells are potential targets. One of these approaches is the incorporation of molecules capable of interacting with PRRs to recognize PAMPs. TLR is found in APC. The recognition of PAMPs by TLRs can result in the expression of co-stimulation molecules as well as the expression of proinflammatory cytokines, TNF-α, COX-2, and interferon associated with the development of adaptive immune responses by B and T lymphocytes. This project aims to determine the possibility of epitopes from protein AGJ68032.1 to be TB vaccine by comparing the results of docking epitope-TLR2 with TLR2-ESAT6. The material used in this project is protein AGJ68032.1 virulence factor Mce family protein [Mycobacterium tuberculosis str. Beijing/NITR203]. The steps were carried out: search for fasta AGJ68032.1, protein similarity test against Mycobacterium tuberculosis protein, determine the location of proteins, search for protein characteristics, find the location of all proteins, search for Bcell epitope, search for Tcell epitope (MHC class 2), epitope similarity test from MHC class 2 with homo sapiens, antigenecity test, allergenicity test, search for the 3D shape of each epitope-TLR2-ESAT-6, molecular docking TLR2 with ESAT-6 and TLR 2 with epitope and comparing the result data Docking. Epitope protein AGJ68031.1 (FAGDDVRIRGVPVGKIVKIEPQPLRAKVSFW) has high potential to be used as a tuberculosis vaccine candidate because the docking results with TLR have a HADDOCK score of -152.5 +/- 7.3 and an RSMD value that is close to the HADDOCK score and the RSMD TLR2 value with ESAT6.
Desain Vaksin Tuberculosis Secara in Silico Untuk Tuberculosis (TBC) Paruparu Agusinta, Astrid Karindra; Wahjudi, Mariana; Antonius, Yulanda
Syntax Literate Jurnal Ilmiah Indonesia
Publisher : Syntax Corporation

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.36418/syntax-literate.v10i11.62348

Abstract

Tuberculosis (TB) is one of the 10 high mortality diseases and causes the highest number of deaths caused by Mycobacterium bacteria. The BCG vaccine is a vaccine given in an effort to prevent tuberculosis (TB). The BCG vaccine contains a weakened strain of TB bacteria which aims to build immunity and encourage the body to fight TB if infected. However, someone who received the vaccine as a child is still at risk of being infected with TB. So an alternative vaccine is needed for TB. The proteins used were human TLR and ESAT-6 as positive controls. The ESAT -6 protein is a protein excreted by bacteria which plays a role in virulence when in the human body. This research aims to design potential tuberculosis vaccine design candidates in silico. The method used is selection of target epitope sequences using NCBI, Prediction of transmembrane peptide signals using Signal IP 5.0 and TMHMM, prediction of epitope interactions with T cell and B cell receptors using IEDB, analysis of antigenicity and allegenicity, prediction of epitope interactions with T cell and B cell receptors using the molecular docking method, and analysis using PDBsum. The results show that AGJ67874, OBK19877, GLB86787 show that each has the potential to be an alternative vaccine when compared to ESAT-6 as a standard epitope. The closest result is GLB86787.
In Silico Analysis of Non-synonymous Mutations in the durA Gene and Their Effects on the Stability and Physicochemical Properties of Duramycin Ade Prasetya, Yulianto; Kok, Tjie; Wahjudi, Mariana
Tropical Genetics Vol. 5 No. 2 (2025): Genetics
Publisher : Genetikawan Muda Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24036/tg.v5i2.84

Abstract

Duramycin is a lantibiotic peptide encoded by the durA gene, known for its antimicrobial activity against Gram-positive bacteria. This study aimed to evaluate the effects of single-point mutations on the stability and structural integrity of duramycin using a comprehensive in silico approach. Five variants—C1S, F7A, T11Y, D15E, and K19V—were designed and assessed using I-Mutant2.0 to predict their impact on protein stability. ProtParam analysis was conducted to determine molecular weight, isoelectric point (pI), net charge at pH 7, instability index, aliphatic index, and hydropathicity (GRAVY). In addition, PEP-FOLD3 was employed to model the 3D conformations of each mutant peptide. Results showed that K19V improved peptide stability and increased aliphatic index and GRAVY score, indicating enhanced hydrophobicity and potential thermal stability. In contrast, F7A led to a major structural shift marked by an α-helical conformation and reduced stability. C1S and T11Y induced minor destabilizing effects, while D15E offered a moderately stabilizing substitution with minimal structural deviation. Overall, this study highlights the functional relevance of C-terminal and hydrophobic residues in maintaining duramycin’s structural compactness and provides a framework for future design of optimized antimicrobial peptides through rational mutation