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Antihypertensive Effect of Rice Bran Derived Amino Acids Through Modulation of iNOS Expression and Renal Histopathology in DOCA Salt Induced Hypertensive Rats Muhammad Fikri Nur; Devi Ramadani; Muh Fikry Baharuddin; Almas Dwi Khairana; Saidun Fiddaroini; Akhmad Sabarudin; Anna Safitri; Wibi Riawan; Dyah Kinasih Wuragil; Hilman Nurmahdi; Aulanni'am Aulanni'am
Jurnal Penelitian Pendidikan IPA Vol 12 No 1 (2026)
Publisher : Postgraduate, University of Mataram

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29303/jppipa.v12i1.13491

Abstract

Hypertension is a major global health concern and a leading risk factor for cardiovascular mortality. Conventional treatment with ACE inhibitors like captopril is effective but often causes adverse effects including cough, dizziness, and renal impairment. This study evaluated the antihypertensive effects of rice bran in DOCA-salt-induced hypertensive rats. In vitro analysis revealed 45.58% soluble fiber and rich amino acid content, including 2.121 mg L-Arginine, a nitric oxide precursor promoting vasodilation. Male Wistar rats were divided into five groups: negative control, positive control, captopril treatment (5 mg/kg BW), and rice bran supplementation at 1% and 2% of 25 g feed. The 2% rice bran group significantly (p < 0.05) reduced renal iNOS expression by 88.32% compared to hypertensive controls, surpassing captopril's 22.96% reduction. Histopathological examination revealed notable renal protection with complete absence of fatty degeneration and minimal glomerular inflammation in the 2% rice bran group. These findings demonstrate potent antihypertensive activity through ACE inhibition, enhanced nitric oxide bioavailability, and mitigation of oxidative and inflammatory stress, establishing rice bran as a promising natural therapeutic alternative for hypertension management
Structural Characterization and Immunogenic Evaluation of a 50 kDa Thyroid Peroxidase Fraction Isolated from Hypothyroid Patient Serum Devi Ramadani; Aulanni&#039;am Aulanni&#039;am; Muh. Fikry Baharuddin; Almas Dwi Khairana; Saidun Fiddaroini; Muhammad Fikri Nur; Hilman Nurmahdi; Wibi Riawan; Arie Srihardyastutie; Akhmad Sabarudin; Dyah Kinasih Wuragil; Rulli Rosandi; Achmad Rudijanto; Ahmad Lubab
Science and Technology Indonesia Vol. 11 No. 4 (2026): October
Publisher : Research Center of Inorganic Materials and Coordination Complexes, FMIPA Universitas Sriwijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.26554/sti.2026.11.4.1476-1496

Abstract

Thyroid peroxidase (TPO) is a key enzyme involved in thyroid hormone biosynthesis and one of the major autoantigens in autoimmune thyroid disease. However, studies investigating immunoreactive serum-derived TPO-related protein fractions remain limited. This study aimed to isolate an approximately 50 kDa immunoreactive protein fraction from the serum of hypothyroid patients, characterize its biochemical properties, and evaluate its immunogenicity for rabbit polyclonal antibody production. Serum samples were initially characterized based on anti-TPO antibody levels and total protein concentration. Rabbits were immunized with the isolated protein, and the resulting immune response was evaluated by indirect ELISA, SDS-PAGE, Western blotting, histopathology, and immunohistochemistry. SDS-PAGE consistently revealed a distinct protein band at approximately 50 kDa. ATR-FTIR analysis demonstrated characteristic protein-associated functional groups, while LC-MS/MS confirmed the proteinaceous nature of the isolated fraction through amino acid composition analysis. Immunization induced a progressive increase in anti-TPO IgG levels, and the purified rabbit IgG exhibited the expected electrophoretic profile under reducing and non-reducing conditions. Western blot analysis demonstrated that the generated polyclonal antibodies recognized the isolated approximately 50 kDa protein fraction, whereas no signal was detected in the secondary antibody-only control. Histopathological and immunohistochemical analyses further supported activation of the immune response following immunization. These findings demonstrate that the isolated approximately 50 kDa immunoreactive protein fraction possesses biochemical and immunogenic properties and has potential as an experimental immunogen for polyclonal antibody production.