Evidence map›Paper›PMID 23778121›Full record

ArticleMolecules (Basel, Switzerland)2013

Novel antimicrobial peptide dendrimers with amphiphilic surface and their interactions with phospholipids--insights from mass spectrometry.

Piotr Polcyn, Paulina Zielinska, Magdalena Zimnicka, Anna Troć, Przemysław Kalicki, Jolanta Solecka, Anna Laskowska, Zofia Urbanczyk-Lipkowska

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.2field-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

7 citing papers in PubMed, 19 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

8 authors at 2 institutions in 1 country.

Piotr PolcynInstitute of Organic Chemistry PAS, Kasprzaka Str. 44/54, Warsaw 01-224, Poland.
Paulina Zielinska
Magdalena Zimnicka
Anna Troć
Przemysław Kalicki
Jolanta Solecka
Anna Laskowska
Zofia Urbanczyk-Lipkowska
Institute of Organic Chemistry · PLNational Institute of Public Health · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A series of new peptide dendrimers with amphiphilic surface, designed around a dendronized ornithine (Orn) core were synthesized and characterized by ESI-MS, ¹H-, ¹³C- NMR, and CD spectrometry. An improved antimicrobial potency against S. aureus and E. coli was detected as a result of an increased charge, higher branching and variable lipophilicity of the residues located at the C-terminus. Minimal inhibitory concentration (MIC) values indicated that the selected dendrimers were not sensitive to the physiological concentration of Na⁺ and K⁺ ions (100 mM), but expressed reduced potency at 10 mM concentration of Mg²⁺ and Ca²⁺ ions. Circular dichroism (CD) curves measured under various conditions revealed structure and solvent-dependent curve evolution. ESI-MS studies of gas-phase interactions between selected dendrimers and both anionic (DMPG) and neutral (DMPC) phospholipids revealed the presence of variously charged dendrimer/phospholipid aggregates with 1:1 to 1:5 stoichiometry. The collision-induced fragmentation (CID) of the most abundant [dendrimer/phospholipid]²⁺ ions of the 1:1 stoichiometry demonstrated that the studied dendrimers formed stronger complexes with anionic DMPG. Both phospholipids have higher affinity towards dendrimers with a more compact structure. Higher differences in CID energy necessary for dissociation of 50% of the complex formed by dendrimers with DMPG vs. DMPC (ΔCID₅₀) correlate with a lower hemotoxicity. Mass spectrometry results suggest that for a particular group of compounds the ΔCID₅₀ might be one of the important factors explaining selectivity of antimicrobial peptides and their branched analogs targeting the bacterial membrane. Both circular dichroism and mass spectrometry studies demonstrated that dendrimers of N(α)- and N(ε)-series possess a different conformation in solution and different affinity to model phospholipids, what might influence their specific microbicidal mechanism.

Indexed as

Antimicrobial Cationic PeptidesCircular DichroismDendrimersErythrocytesHemolysisHydrophobic and Hydrophilic InteractionsMass SpectrometryMicrobial Sensitivity TestsMolecular StructurePhospholipidsAntimicrobial Cationic PeptidesDendrimersPhospholipids

Identifiers

PMID23778121
PMCPMC6270063
OpenAlexW2130553306

What OpenQuestion holds

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LicenceCC BY
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.