{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T07:26:58Z","timestamp":1767166018009,"version":"build-2238731810"},"reference-count":25,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T00:00:00Z","timestamp":1684800000000},"content-version":"vor","delay-in-days":142,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100020912","name":"King Faisal University","doi-asserted-by":"publisher","award":["GRANT3230"],"award-info":[{"award-number":["GRANT3230"]}],"id":[{"id":"10.13039\/501100020912","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["BioMed Research International"],"published-print":{"date-parts":[[2023,1]]},"abstract":"<jats:p>Lactoferrin (LF) is a major natural antimicrobial agent secreted in body fluids as a natural innate immunity protein. The action and structure of LF are closely related to its iron\u2010binding capacity with structural reporting in open and closed conformations. This study looked at how lactoferrin structures change in camel (cLF), bovine (bLF), and human (hLF) lactoferrin closed forms after iron is removed from their binding sites. Initially, the sequence comparison between cLF and the LFs of marine mammals, bats, and domestic animals was the most intriguing conclusion. Camel LF is revealed to be more closely related to marine animals (~80.36% identity) and bats (~79.3% identity) than to terrestrial mammal species (~75.5% identity). Results indicated that cLF was more dynamic in nature than bLF and hLF by showing higher RMSD values. The cLF is known to be half lactoferrin half transferrin; in this study, we show that there are different MD behavior of both iron\u2010binding sites. While LF contains two lobes (C\u2010 and N\u2010lobes), the C\u2010lobe showed high fluctuations as N\u2010lobe was more stable in the absence of ferric ions. The C\u2010lobe and N\u2010lobe of cLF react differently at physiological pH, revealing distinct molecular interactions between these components. In addition, cLF showed higher system flexibility derived from its larger RMSD, RMSF, lower intermolecular hydrogen bonds, and higher solvent accessible surface area (SASA).<\/jats:p>","DOI":"10.1155\/2023\/2322286","type":"journal-article","created":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T15:20:08Z","timestamp":1684855208000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["[Retracted] The Antimicrobial Bifunctional Camel Lactoferrin: In Silico and Molecular Dynamic Perspective"],"prefix":"10.1155","volume":"2023","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7706-821X","authenticated-orcid":false,"given":"Maathir N.","family":"Alhumam","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6738-967X","authenticated-orcid":false,"given":"Naser","family":"Alhumam","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3668-5147","authenticated-orcid":false,"given":"Mahmoud","family":"Kandeel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2023,5,23]]},"reference":[{"key":"e_1_2_9_1_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00203-020-01964-2"},{"key":"e_1_2_9_2_2","doi-asserted-by":"publisher","DOI":"10.2217\/fvl-2020-0170"},{"key":"e_1_2_9_3_2","doi-asserted-by":"publisher","DOI":"10.1139\/bcb-2020-0035"},{"key":"e_1_2_9_4_2","doi-asserted-by":"publisher","DOI":"10.1186\/s12917-019-2067-6"},{"key":"e_1_2_9_5_2","doi-asserted-by":"publisher","DOI":"10.3390\/microorganisms10010110"},{"key":"e_1_2_9_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/172.2.380"},{"key":"e_1_2_9_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.virol.2005.01.010"},{"key":"e_1_2_9_8_2","doi-asserted-by":"publisher","DOI":"10.1007\/s007050070077"},{"key":"e_1_2_9_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/jmv.10337"},{"key":"e_1_2_9_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.antiviral.2004.05.005"},{"key":"e_1_2_9_11_2","doi-asserted-by":"publisher","DOI":"10.1007\/s004300050049"},{"key":"e_1_2_9_12_2","volume-title":"Bovine lactoferrin activity against chikungunya and Zika viruses","author":"Carvalho C. 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