دورية أكاديمية

Structural dynamics influences the antibacterial activity of a cell-penetrating peptide (KFF)3K

التفاصيل البيبلوغرافية
العنوان: Structural dynamics influences the antibacterial activity of a cell-penetrating peptide (KFF)3K
المؤلفون: Julia Macyszyn, Piotr Chyży, Michał Burmistrz, Małgorzata Lobka, Joanna Miszkiewicz, Monika Wojciechowska, Joanna Trylska
المصدر: Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
بيانات النشر: Nature Portfolio, 2023.
سنة النشر: 2023
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Abstract Given the widespread demand for novel antibacterial agents, we modified a cell-penetrating peptide (KFF)3K to transform it into an antibacterial peptide. Namely, we inserted a hydrocarbon staple into the (KFF)3K sequence to induce and stabilize its membrane-active secondary structure. The staples were introduced at two positions, (KFF)3K[5–9] and (KFF)3K[2–6], to retain the initial amphipathic character of the unstapled peptide. The stapled analogues are protease resistant contrary to (KFF)3K; 90% of the stapled (KFF)3K[5–9] peptide remained undigested after incubation in chymotrypsin solution. The stapled peptides showed antibacterial activity (with minimal inhibitory concentrations in the range of 2–16 µM) against various Gram-positive and Gram-negative strains, contrary to unmodified (KFF)3K, which had no antibacterial effect against any strain at concentrations up to 32 µM. Also, both stapled peptides adopted an α-helical structure in the buffer and micellar environment, contrary to a mostly undefined structure of the unstapled (KFF)3K in the buffer. We found that the antibacterial activity of (KFF)3K analogues is related to their disruptive effect on cell membranes and we showed that by stapling this cell-penetrating peptide, we can induce its antibacterial character.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2045-2322
Relation: https://doaj.org/toc/2045-2322
DOI: 10.1038/s41598-023-38745-y
URL الوصول: https://doaj.org/article/4620ee9ebd454de4b5937be53bc5b2bf
رقم الأكسشن: edsdoj.4620ee9ebd454de4b5937be53bc5b2bf
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20452322
DOI:10.1038/s41598-023-38745-y