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This study evaluated the antifungal potential of a newly designed MAF\u20101A\u2010derived peptide against\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>C. parapsilosis<\/jats:italic>\n                    <\/jats:styled-content>\n                    . Four derivatives were chemically synthesized and structurally characterized. Our hybrid method included the use of computational tools for hydrophobic optimization, amphipathic \u03b1\u2010helix stabilization, and peptide\u2010membrane interaction prediction together with experimental validations. We synthesized four designed derivatives (8KGF7, 9GIF6, 10KLF6, and 10GIF6) by Fmoc\u2010based solid\u2010phase chemistry. Its antifungal activity against\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>C. parapsilosis<\/jats:italic>\n                    <\/jats:styled-content>\n                    was assessed using the broth microdilution assay. Trypsin stability was evaluated by incubating 10KLF6 with trypsin followed by measurement of residual antifungal activity. Hemolytic safety was assessed using human red blood cells via hemolytic activity assays. The results demonstrated that 10KLF6 exhibited up to 15\u2010fold higher antifungal activity against\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>C. parapsilosis<\/jats:italic>\n                    <\/jats:styled-content>\n                    compared to MAF\u20101A. Additionally, 10KLF6 retained more than 20% of its antifungal activity after 100\u2009min of trypsin digestion and showed low hemolytic toxicity. Collectively, 10KLF6 possesses potent antifungal activity as well as favorable stability and safety profiles against\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>C. parapsilosis<\/jats:italic>\n                    <\/jats:styled-content>\n                    , which supports its further exploration as a promising candidate for the development of potent and stable antifungal peptide agents.\n                  <\/jats:p>","DOI":"10.1002\/psc.70127","type":"journal-article","created":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T12:40:46Z","timestamp":1790944846000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["In Vitro Assessment of a MAF\u20101A\u2010Derived Peptide Against\n                    <scp>\n                      <i>Candida parapsilosis<\/i>\n                    <\/scp>\n                    : Antifungal Potency, Trypsin Stability, and Hemolytic Safety"],"prefix":"10.1002","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-6858-1078","authenticated-orcid":false,"given":"Mei","family":"Tao","sequence":"first","affiliation":[{"name":"Guizhou University Medical College  Guiyang Guizhou Province China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-2343-2358","authenticated-orcid":false,"given":"Runze","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Cardiovascular Medicine The Affiliated Hospital of Guizhou Medical University  Guiyang Guizhou Province China"},{"name":"The Key Laboratory of Myocardial Remodeling Research The Affiliated Hospital of Guizhou Medical University  Guiyang Guizhou Province China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9298-2239","authenticated-orcid":false,"given":"Fangfang","family":"Hu","sequence":"additional","affiliation":[{"name":"Department of Clinical 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