Tejo, Bimo Ario
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Antifreeze Proteins: Characteristics and Potential Applications Tejo, Bimo Ario; Asmawi, Azren Aida; Rahman, Mohd Basyaruddin Abdul
Makara Journal of Science Vol. 24, No. 1
Publisher : UI Scholars Hub

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Abstract

The freezing of water is usually fatal to most organisms because it causes extensive damage to cell membranes due to the formation of ice crystals. However, several structurally different classes of antifreeze proteins (AFPs) found in fish, insects, plants, and microorganisms, including bacteria, yeast, and fungi, have been found to be capable of modifying the growth of ice crystals by thermal hysteresis and ice recrystallization inhibition. This unique property could potentially be applied to medicine and the industry as it is useful when low-temperature storage is required and ice crystallization must be avoided. However, the application of AFPs today is not economically viable due to the complexity of the large proteins, the laborious procedures required, and the low yields obtained. A wide range of peptides mimicking their parent proteins were recently successfully designed and chemically synthesized. The developed approaches present new opportunities to understand the structure–function relationship of small-structured peptides with antifreeze properties. This mini-review highlights the diversity, classification, and properties of AFPs. The emerging applications of short mimetic peptides of AFPs and their potential application are also described.
EVALUATION AND INHIBITORY MECHANISM ANALYSIS OF NATURAL COMPOUNDS AGAINTS DIHYDROOROTATE DEHYDROGENASE AS ANTI-CANCER AGENTS Wibowo, Aji; Waluyo, Danang; Tejo, Bimo Ario; Komariyah, Tinta; Besari, Ariza Yandwiputra; Prabandari, Erwahyuni Endang
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol. 10 No. 2 (2023)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/jbbi.2023.2842

Abstract

Cancer remains one of the deadliest diseases worldwide, and currently cancer treatment is facing several problems related to adverse effects and drug resistance. To address these problems, new prospective anticancer medications are required. Natural compounds, which have been extensively used in the drug research, including for the treatment of cancer, are emerging as viable candidates. This study aimed to evaluate 33 in-house natural compounds against dihydroorotate dehydrogenase (DHODH) enzyme, a viable target to develop anticancer agent, and to analyze the hit inhibitory mechanism against protein target. In the activity assay, atovaquone was the sole substance to have activity against DHODH, with an inhibition rate of 47.44% at 10 µM. However, discrepancies were shown in the molecular docking result, where atovaquone were identified as hits. Molecular dynamic analysis revealed that atovaquone initially bound to the active site before being forced to the outside due to cleavage of hydrogen bond between the ligand and responsible residue. This study clearly demonstrated the importance of molecular dynamic analysis to study inhibitory mechanism of compound against target protein that may be useful for further development.