Evidence map›Paper›PMID 26745958›Full record

ArticleEuropean biophysics journal : EBJ2016

The effect of amidation on the behaviour of antimicrobial peptides.

Manuela Mura, Jianping Wang, Yuhua Zhou, Marco Pinna, Andrei V Zvelindovsky, Sarah R Dennison, David A Phoenix

Open access · hybridAbstract read
In one paragraph

Article in European biophysics journal : EBJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 111 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

7 authors at 4 institutions in 2 countries.

Manuela MuraComputational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK. mmura@lincoln.ac.uk.ORCID http://orcid.org/0000-0002-3913-7595
Jianping WangUCLan Biomedical Technology Limited (Shenzhen), Shenzhen Virtual University Park, Shenzhen, 518057, People's Republic of China.
Yuhua ZhouUCLan Biomedical Technology Limited (Shenzhen), Shenzhen Virtual University Park, Shenzhen, 518057, People's Republic of China.
Marco PinnaComputational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
Andrei V ZvelindovskyComputational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
Sarah R DennisonSchool of Pharmacy and Biomedical Science, University of Central Lancashire, Preston, PR1 2HE, UK.
David A PhoenixSchool of Applied Science, London South Bank University, 103 Borough Road, London, SE1 0AA, UK.
University of Lincoln · GBShenzhen Technology University · CNLondon South Bank University · GBUniversity of Lancashire · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aurein 2.6-COOH and aurein 3.1-COOH were studied along with their naturally occurring C-terminally amidated analogues. Circular dichroism (CD) and molecular dynamic (MD) simulations were used to study the effects of amidation on the interaction of antimicrobial peptides (AMPs) with lipid bilayers. CD measurements and MD analysis suggested that both peptide analogues were predominantly random coil and adopted low levels of α-helical structure in solution (<30%) and in the presence of a lipid bilayer the peptides formed a stable α-helical structure. In general, amidated analogues have a greater propensity than the non-amidated peptides to form a α-helical structure. MD simulations predicted that aurein 2.6-COOH and aurein 3.1-CHOOH destabilised lipid bilayers from 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-glycero-3-phosphoserine via angled bilayer penetration. They also showed that aurein 2.6-CONH₂ and aurein 3.1-CONH₂ formed a helix horizontal to the plane of an asymmetric interface.

Indexed as

Molecular Dynamics SimulationAmidesAntimicrobial Cationic PeptidesDimyristoylphosphatidylcholineLipid BilayersAmidesAntimicrobial Cationic PeptidesDimyristoylphosphatidylcholineLipid BilayersAmino acidAnticancerAntimicrobial peptidesCooperative effectMembraneMolecular dynamicsSecondary structure

Identifiers

PMID26745958
PMCPMC4796345
OpenAlexW2231559741

What OpenQuestion holds

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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.