Evidence map›Paper›PMID 29131929›Full record

ArticleChemphyschem : a European journal of chemical physics and physical chemistry2018

Insights on the Structure, Molecular Weight and Activity of an Antibacterial Protein-Polymer Hybrid.

Yanxiong Pan, Sunanda Neupane, Jasmin Farmakes, Myungkeun Oh, Kylie Bentz, Yongki Choi, Zhongyu Yang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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.

Yanxiong PanDepartment of Chemistry and Biochemistry, North Dakota State University, 1231 Albrecht Blvd, Fargo, ND, 58108, USA.
Sunanda NeupaneDepartment of Chemistry and Biochemistry, North Dakota State University, 1231 Albrecht Blvd, Fargo, ND, 58108, USA.
Jasmin FarmakesDepartment of Chemistry and Biochemistry, North Dakota State University, 1231 Albrecht Blvd, Fargo, ND, 58108, USA.
Myungkeun OhMaterials and Nanotechnology Program, North Dakota State University, 51 Batcheller Technology Center, Fargo, ND, 58105, USA.
Kylie BentzDepartment of Chemistry and Biochemistry, North Dakota State University, 1231 Albrecht Blvd, Fargo, ND, 58108, USA.
Yongki ChoiMaterials and Nanotechnology Program, North Dakota State University, 51 Batcheller Technology Center, Fargo, ND, 58105, USA.
Zhongyu YangDepartment of Chemistry and Biochemistry, North Dakota State University, 1231 Albrecht Blvd, Fargo, ND, 58108, USA.ORCID 0000-0002-3018-3608

Funding

Developing a hybrid biomolecule nano-circuit approach for observing and manipulating single protein dynamicsR15GM122063 · NIGMS · NORTH DAKOTA STATE UNIVERSITY · PI CHOI, YONGKI · 2016 to 2016
$424k
NIGMS NIH HHS R15 GM122063
6 · The paper itself

Abstract

Protein-polymer conjugates are attractive biomaterials which combine the functions of both proteins and polymers. The bioactivity of these hybrid materials, however, is often reduced upon conjugation. It is important to determine and monitor the protein structure and active site availability in order to optimize the polymer composition, attachment point, and abundance. The challenges in probing these insights are the large size and high complexity in the conjugates. Herein, we overcome the challenges by combining electron paramagnetic resonance (EPR) spectroscopy and atomic force microscopy (AFM) and characterize the structure of antibacterial hybrids formed by polyethylene glycol (PEG) and an antibacterial protein. We discovered that the primary reasons for activity loss were PEG blocking the substrate access pathway and/or altering protein surface charges. Our data indicated that the polymers tended to stay away from the protein surface and form a coiled conformation. The structural insights are meaningful for and applicable to the rational design of future hybrids.

Indexed as

Anti-Bacterial AgentsBiocompatible MaterialsCatalytic DomainElectron Spin Resonance SpectroscopyMacromolecular SubstancesMicrococcusMicroscopy, Atomic ForceMolecular WeightMuramidasePolyethylene GlycolsProtein Structure, SecondaryAnti-Bacterial AgentsBiocompatible MaterialsMacromolecular SubstancesMuramidasePolyethylene GlycolsAFMbiophysicsEPR spectroscopyPEGylated proteinstructure-activity relationship

Identifiers

PMID29131929
PMCPMC6122959

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.