{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T11:56:37Z","timestamp":1782561397221,"version":"3.54.5"},"reference-count":38,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2025,9,21]],"date-time":"2025-09-21T00:00:00Z","timestamp":1758412800000},"content-version":"vor","delay-in-days":263,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2025,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>The rise of multidrug\u2010resistant <jats:styled-content style=\"fixed-case\"><jats:italic>Streptococcus pneumoniae<\/jats:italic><\/jats:styled-content> poses a major public health threat, necessitating novel therapeutic targets. Pneumococcal Surface Adhesin A (PsaA), a conserved surface lipoprotein, plays a key role in manganese acquisition, colonization and virulence. Immunization with PsaA elicits protective immunity, while fragment\u2010based drug design has identified inhibitors disrupting its function. PsaA emerges as a promising molecular target for innovative therapeutic strategies against pneumococcal diseases. Antimicrobial peptides (AMPs) are crucial components of the innate immune system, providing a potent defence mechanism against a broad spectrum of pathogens. Moricin, an AMP initially identified in <jats:styled-content style=\"fixed-case\"><jats:italic>Bombyx mori<\/jats:italic><\/jats:styled-content>, exhibits robust antimicrobial activity against Gram\u2010positive bacteria. This study explores the inhibitory effects of moricin on <jats:styled-content style=\"fixed-case\"><jats:italic>S.\u2009pneumoniae<\/jats:italic><\/jats:styled-content>, a significant human pathogen responsible for severe infections such as pneumonia, meningitis and sepsis. In silico analyses, including molecular docking and molecular dynamics simulations, revealed a strong interaction between moricin and the PsaA. In\u00a0vitro studies corroborated the computational findings, demonstrating a dose\u2010dependent inhibition of <jats:styled-content style=\"fixed-case\"><jats:italic>S.\u2009pneumoniae<\/jats:italic><\/jats:styled-content> growth. Moricin induced bacterial membrane disruption, evidenced by increased membrane permeability, release of intracellular contents and altered membrane potential, highlighting the bactericidal mode of action. Furthermore, time\u2010kill kinetics revealed rapid bacterial eradication, underscoring moricin's efficacy. Additionally, toxicity assays on the macrophage BV2 cell line demonstrated that moricin caused no significant structural or organelle damage, emphasizing its biocompatibility and safety. The integration of in silico and in\u00a0vitro approaches provides comprehensive mechanistic insights into moricin's antimicrobial action and establishes its potential as a safe and effective therapeutic agent against <jats:styled-content style=\"fixed-case\"><jats:italic>S.\u2009pneumoniae<\/jats:italic><\/jats:styled-content>.<\/jats:p>","DOI":"10.1002\/psc.70055","type":"journal-article","created":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T00:40:48Z","timestamp":1758501648000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Antimicrobial Peptide Moricin Inhibits <scp><i>Streptococcus pneumoniae<\/i><\/scp> Growth Through Membrane Disruption: Insights From In Silico and In\u00a0Vitro Studies"],"prefix":"10.1002","volume":"31","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7764-534X","authenticated-orcid":false,"given":"Imran","family":"Ahmad","sequence":"first","affiliation":[{"name":"Department of 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