Evidence map›Paper›PMID 26508857›Full record

ArticleInternational journal of nanomedicine2015

Design and activity of a cyclic mini-β-defensin analog: a novel antimicrobial tool.

Olga Scudiero, Ersilia Nigro, Marco Cantisani, Irene Colavita, Marilisa Leone, Flavia Anna Mercurio, Massimiliano Galdiero, Antonello Pessi, Aurora Daniele, Francesco Salvatore and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of nanomedicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 40 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Olga ScudieroCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy ; Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli Federico II, Naples, Italy.
Ersilia NigroCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy.
Marco CantisaniDipartimento di Farmacia, Università di Napoli Federico II, Naples, Italy.
Irene ColavitaCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy.
Marilisa LeoneIstituto di Biostrutture e Bioimmagini, CNR, Naples, Italy.
Flavia Anna MercurioIstituto di Biostrutture e Bioimmagini, CNR, Naples, Italy.
Massimiliano GaldieroDipartimento di Medicina Sperimentale, Seconda Università di Napoli, Naples, Italy.
Antonello PessiCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy.
Aurora DanieleCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy ; Dipartimento di Scienze e Tecnologie Ambientali Biologiche Farmaceutiche, Seconda Università di Napoli, Caserta, Italy.
Francesco SalvatoreCEINGE-Biotecnologie Avanzate Scarl, Naples, Italy ; Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli Federico II, Naples, Italy ; IRCCS Fondazione SDN, Naples, Italy.
Stefania GaldieroDipartimento di Farmacia, Università di Napoli Federico II, Naples, Italy ; Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy.
Ceinge Biotecnologie Avanzate (Italy) · ITInstitute of Biostructure and Bioimaging · ITUniversity of Naples Federico II · ITSDN Istituto di Ricerca Diagnostica e Nucleare · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have designed a cyclic 17-amino acid β-defensin analog featuring a single disulfide bond. This analog, designated "AMC" (ie, antimicrobial cyclic peptide), combines the internal hydrophobic domain of hBD1 and the C-terminal charged region of hBD3. The novel peptide was synthesized and characterized by nuclear magnetic resonance spectroscopy. The antimicrobial activities against gram-positive and gram-negative bacteria as well as against herpes simplex virus type 1 were analyzed. The cytotoxicity and serum stability were assessed. Nuclear magnetic resonance of AMC in aqueous solution suggests that the structure of the hBD1 region, although not identical, is preserved. Like the parent defensins, AMC is not cytotoxic for CaCo-2 cells. Interestingly, AMC retains the antibacterial activity of the parent hBD1 and hBD3 against Pseudomonas aeruginosa, Enterococcus faecalis, and Escherichia coli, and exerts dose-dependent activity against herpes simplex virus type 1. Moreover, while the antibacterial and antiviral activities of the oxidized and reduced forms of the parent defensins are similar, those of AMC are significantly different, and oxidized AMC is also considerably more stable in human serum. Taken together, our data also suggest that this novel peptide may be added to the arsenal of tools available to combat antibiotic-resistant infectious diseases, particularly because of its potential for encapsulation in a nanomedicine vector.

Indexed as

Drug DesignAmino Acid SequenceAnti-Bacterial AgentsAntiviral AgentsBacteriabeta-DefensinsCaco-2 CellsDisulfidesDose-Response Relationship, DrugDrug StabilityHerpesvirus 1, HumanHumansMolecular Sequence DataAnti-Bacterial AgentsAntiviral Agentsbeta-DefensinsDisulfidesantimicrobial activitycyclic mini-peptidehuman beta-defensin

Identifiers

PMID26508857
PMCPMC4610797
OpenAlexW2157511732

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.