{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T19:42:17Z","timestamp":1789846937799,"version":"4.0.1"},"reference-count":59,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2015,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            We have designed a hybrid peptide by combining sequences of human \u03b2-defensin-1 (HBD-1) and \u03b8-defensin, in an attempt to generate a molecule that combines the diversity in structure and biological activity of two different peptides to yield a promising therapeutic candidate. HBD-1 was chosen as it is a natural defensin of humans that is constitutively expressed, but its antibacterial activity is considerably impaired by elevated ionic strength. \u03b8-Defensins are expressed in human bone marrow as a pseudogene and are homologous to rhesus monkey circular minidefensins. Retrocyclins are synthetic human \u03b8-defensins. The cyclic nature of the \u03b8-defensin peptides makes them salt resistant, nonhemolytic, and virtually noncytotoxic\n            <jats:italic>in vitro<\/jats:italic>\n            . However, a nonhuman circular molecule developed for clinical use would be less viable than a linear molecule. In this study, we have fused the C-terminal region of HBD-1 to the nonapeptide sequence of a synthetic retrocyclin. Cyclization was achieved by joining the terminal ends of the hybrid peptide by a disulfide bridge. The hybrid peptide with or without the disulfide bridge exhibited enhanced antimicrobial activity against both Gram-negative and Gram-positive bacteria as well as against fungi, including clinical bacterial isolates from eye infections. The peptide retained activity in the presence of NaCl and serum and was nonhemolytic\n            <jats:italic>in vitro<\/jats:italic>\n            . Thus, the hybrid peptide generated holds potential as a new class of antibiotics.\n          <\/jats:p>","DOI":"10.1128\/aac.03901-14","type":"journal-article","created":{"date-parts":[[2014,10,28]],"date-time":"2014-10-28T05:13:34Z","timestamp":1414473214000},"page":"217-225","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["A Hybrid Cationic Peptide Composed of Human \u03b2-Defensin-1 and Humanized \u03b8-Defensin Sequences Exhibits Salt-Resistant Antimicrobial Activity"],"prefix":"10.1128","volume":"59","author":[{"given":"Sudar","family":"Olli","sequence":"first","affiliation":[{"name":"CSIR-Centre for Cellular and Molecular Biology, Hyderabad, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ramakrishnan","family":"Nagaraj","sequence":"additional","affiliation":[{"name":"CSIR-Centre for Cellular and Molecular Biology, Hyderabad, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Swapna R.","family":"Motukupally","sequence":"additional","affiliation":[{"name":"Jhaveri Microbiology Centre, L. 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