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      In vitro and in vivo antimicrobial activity of two α-helical cathelicidin peptides and of their synthetic analogs

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          Abstract

          Two α-helical antimicrobial peptides (BMAP-27 and -28) and four synthetic analogs were compared for in vitro and in vivo antimicrobial efficacy. All peptides proved active in vitro at micromolar concentrations against a range of clinical isolates, including antibiotic-resistant strains. BMAP-27 and two analogs were more effective towards Gram-negative, and BMAP-28 towards Gram-positive organisms. In addition, BMAP-28 provided some protection in vitro against human herpes simplex virus type 1 (HSV-1). The parent peptides and mBMAP-28 analog protected mice from lethal i.p. infections in an acute peritonitis model at peptide doses significantly lower than those toxic to the animals, suggesting a satisfactory therapeutic index.

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          Spectroscopic determination of tryptophan and tyrosine in proteins.

          Harold Edelhoch (1967)
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            Rapid and automated tetrazolium-based colorimetric assay for the detection of anti-HIV compounds.

            Rudi Pauwels, Jan Balzarini, Masanori Baba … (1988)
            A rapid, sensitive and automated assay procedure was developed for the in vitro evaluation of anti-HIV agents. An HTLV-I transformed T4-cell line, MT-4, which was previously shown by Koyanagi et al. (1985) to be highly susceptible to, and permissive for, HIV infection, served as the target cell line. Inhibition of the HIV-induced cytopathic effect was used as the end point. The viability of both HIV- and mock-infected cells was assessed spectrophotometrically via the in situ reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT). The procedure was optimized as to make optimal use of multichannel pipettes, microprocessor-controlled dispensing and optical density reading. The absorbance ratio of the mock-infected control to the HIV-infected samples was about 20. This allowed an accurate determination of the 50% effective doses, as demonstrated for 3'-azido-2',3'-dideoxythymidine (AZT), 2',3'-dideoxycytidine (ddCyd), dextran sulfate and heparin. The technique significantly reduced labor time as compared to the trypan blue exclusion method, and permits the evaluation of large numbers of compounds for their anti-HIV activity.
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              Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain.

              Russell D. Romeo, M. Zanetti, A R Gennaro (1995)
              A novel protein family, showing a conserved proregion and a variable C-terminal antimicrobial domain, and named cathelicidin, has been identified in mammalian myeloid cells. The conserved proregion shows sequence similarity to members of the cystatin superfamily of cysteine proteinase inhibitors. Cathelicidins are stored in the cytoplasmic granules of neutrophil leukocytes and release the antimicrobial peptides upon leukocyte activation. Some of these peptides can assume an alpha-helical conformation, others contain one or two disulfide bonds, still others are Pro- and Arg-rich, or Trp-rich. In addition to bacterial killing, some of these peptides exert additional functions related to host defense such as LPS-neutralization and promotion of wound healing.
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                Author and article information

                Contributors
                Margherita Zanetti
                Journal
                Journal ID (nlm-ta): Peptides
                Journal ID (iso-abbrev): Peptides
                Title: Peptides
                Publisher: Elsevier Inc.
                ISSN (Print): 0196-9781
                ISSN (Electronic): 1873-5169
                Publication date PMC-release: 20 December 2003
                Publication date (Print): November 2003
                Publication date (Electronic): 20 December 2003
                Volume: 24
                Issue: 11
                Pages: 1723-1731
                Affiliations
                [a ]Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri, 1, I-34127 Trieste, Italy
                [b ]Department of Sciences and Medical Technologies, University of Udine, P.le Kolbe, 4, I-33100 Udine, Italy
                [c ]Division of Applied Physiology, Institute of Veterinary Physiology, University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland
                [d ]National Laboratory C.I.B., AREA Science Park, I-34012 Padriciano-Trieste, Italy
                Author notes
                [* ]Corresponding author. Tel.: +39-0432-494-390; fax: +39-0432-494-301. zanetti@ 123456icgeb.trieste.it
                [1]

                These authors contributed equally to this work.

                Article
                Publisher ID: S0196-9781(03)00346-2
                DOI: 10.1016/j.peptides.2003.07.025
                PMC ID: 7124310
                PubMed ID: 15019203
                SO-VID: fb46681d-6ddc-467c-a17a-979fb3d535d4
                Copyright statement: Copyright © 2003 Elsevier Inc. All rights reserved.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 1 April 2003
                Date accepted : 2 July 2003
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Keywords: cathelicidin peptide,α-helical antimicrobial peptide,synthetic analog,antimicrobial activity,clinical isolate,in vivo protection,infection
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: cathelicidin peptide, α-helical antimicrobial peptide, synthetic analog, antimicrobial activity, clinical isolate, in vivo protection, infection

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