{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T21:09:42Z","timestamp":1768597782812,"version":"3.49.0"},"reference-count":14,"publisher":"Walter de Gruyter GmbH","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,11,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec id=\"j_jbcpp-2019-0282_s_999_w2aab3b8c96b1b7b1aab1c14b1Aa\">\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>\n                      PBP2a is a type of penicillin-binding proteins (PBPs) that cause resistivity in methicillin-resistant\n                      <jats:italic>Staphylococcus aureus<\/jats:italic>\n                      (MRSA) from \u03b2-lactam antibiotics. MRSA susceptible with cefttobiprole (fifth generation of cephalosporin as an anti-MRSA agent) which inhibits PBP2a and stops its growth. Contrary to its efficacy, ceftobiprole causes taste disturbance more than any other cephalosporins; furthermore, its mechanism is unknown. This study aims to explore an\n                      <jats:italic>in silico<\/jats:italic>\n                      study of a natural compound, which serves as a potential alternative to overcome MRSA with minimum adverse side effects.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_jbcpp-2019-0282_s_998_w2aab3b8c96b1b7b1aab1c14b2Aa\">\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>A molecular docking study was performed using Molegro Virtual Docker version 5.5. Brazilin and proto-sappanins A\u2013E are phytochemical compounds contained in sappan wood extract and are docked into the binding site of PBP2a (Protein Data Bank: ID 4DKI).<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_jbcpp-2019-0282_s_997_w2aab3b8c96b1b7b1aab1c14b3Aa\">\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Brazilin and proto-sappanins A\u2013E have some interaction with Ser 403 amino acid residue which is an important interaction to inhibit PBP2a protein. The result of the molecular docking study showed that the MolDock score of proto-sappanins D and E is lower than that of methicillin but higher than that of its native ligand (ceftobiprole).<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_jbcpp-2019-0282_s_996_w2aab3b8c96b1b7b1aab1c14b4Aa\">\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>The results of this study suggest that proto-sappanins D and E have an excellent potential activity as an alternative to ceftobiprole in limiting MRSA growth through PBP2A enzyme inhibition.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1515\/jbcpp-2019-0282","type":"journal-article","created":{"date-parts":[[2020,1,18]],"date-time":"2020-01-18T10:18:29Z","timestamp":1579342709000},"source":"Crossref","is-referenced-by-count":15,"title":["Molecular docking study of sappan wood extract to inhibit PBP2A enzyme on methicillin-resistant\n                    <i>Staphylococcus aureus<\/i>\n                    (MRSA)"],"prefix":"10.1515","volume":"30","author":[{"given":"Marisca Evalina","family":"Gondokesumo","sequence":"first","affiliation":[{"name":"Department of Biology Pharmacy , Faculty of Pharmacy, University of Surabaya , Jl. Raya Kalirungkut , Surabaya, East Java 60293 , Indonesia , Phone: +62 31 2981110"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ihsan Mulyadi","family":"Kurniawan","sequence":"additional","affiliation":[{"name":"Indonesia University of Education, Department of Biology Education , Bandung, West Java , Indonesia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","published-online":{"date-parts":[[2020,1,18]]},"reference":[{"key":"2025121209201346667_j_jbcpp-2019-0282_ref_001_w2aab3b8c96b1b7b1ab2b2b1Aa","doi-asserted-by":"crossref","unstructured":"Llarrull LI, Fisher JF, Mobashery S. Molecular basis and phenotype of methicillin resistance in Staphylococcus aureus and insights into new \u03b2-lactams that meet the challenge. Antimicrob Agents Chemother 2009;53:4051\u201363.","DOI":"10.1128\/AAC.00084-09"},{"key":"2025121209201346667_j_jbcpp-2019-0282_ref_002_w2aab3b8c96b1b7b1ab2b2b2Aa","doi-asserted-by":"crossref","unstructured":"Waness A. Revisiting methicillin-resistant Staphylococcus aureus infections. J Glob Infect Dis 2010;2:49.","DOI":"10.4103\/0974-777X.59251"},{"key":"2025121209201346667_j_jbcpp-2019-0282_ref_003_w2aab3b8c96b1b7b1ab2b2b3Aa","doi-asserted-by":"crossref","unstructured":"Gajd\u00e1cs M. The continuing threat of methicillin-resistant Staphylococcus aureus. Antibiotics 2010;8:52.","DOI":"10.3390\/antibiotics8020052"},{"key":"2025121209201346667_j_jbcpp-2019-0282_ref_004_w2aab3b8c96b1b7b1ab2b2b4Aa","doi-asserted-by":"crossref","unstructured":"Fishovitz J, Hermoso JA, Chang M, Mobashery S. Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus. IUBMB Life 2014;66:572\u20137.","DOI":"10.1002\/iub.1289"},{"key":"2025121209201346667_j_jbcpp-2019-0282_ref_005_w2aab3b8c96b1b7b1ab2b2b5Aa","doi-asserted-by":"crossref","unstructured":"Foxley MA, Friedline AW, Jensen JM, Nimmo SL, Scull EM, King JB, et al. 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