Identifikasi Mekanisme Molekuler Senyawa Bioaktif Peptida Laut sebagai Kandidat Inhibitor Angiotensin-I Converting Enzyme (ACE)

Main Authors: Fakih, Taufik Muhammad, Dewi, Mentari Luthfika
Format: Article PeerReviewed Book
Bahasa: ind
Terbitan: Universitas Andalas , 2020
Subjects:
Online Access: http://repo.unand.ac.id/36701/1/598-2203-5-PB.pdf
http://repo.unand.ac.id/36701/
http://doi.org/10.25077/jsfk.7.1.76-82.2020
Daftar Isi:
  • Marine peptide bioactive compounds are currently the focus of research because they have unique properties. One important biological roles of these peptide compounds is an antihypertensive agent against Angiotensin-I Converting Enzyme (ACE) activity. There are several peptide compounds that have been proved to inhibit ACE receptors, such as peptide compounds produced by sea cucumbers (Acaudina molpadioides), blue shellfish (Mytilus edulis), and tuna fish (Thunnini). In this research, identification and evaluation of interactions that occur between peptide compounds with ACE receptors were carried out using protein-peptide docking methods. Sequencing of peptide compounds was modeled using PEP-FOLD server. The best conformation was chosen to explore the interaction of ACE receptor macromolecules using PatchDock software. Interactions that occur were observed further using BIOVIA Discovery Studio 2020 software. Based on the results of protein-peptide docking, blue shellfish peptide compounds and tuna fish had a good affinity for the ACE receptor, in which the ACE score were −391.62 kJ/mol and −516.56 kJ/mol, respectively. Thus, the marine peptide bioactive compound is predicted to be a promising candidate for peptidebased ACE receptor inhibitors.