Evidence map›Paper›PMID 34760170›Full record

ArticleChemical science2021

A comprehensive analysis in one run - in-depth conformation studies of protein-polymer chimeras by asymmetrical flow field-flow fractionation.

Bibifatima Kaupbayeva, Hironobu Murata, Krzysztof Matyjaszewski, Alan J Russell, Susanne Boye, Albena Lederer

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Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

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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

6 citing papers in PubMed.

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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

6 authors.

Bibifatima KaupbayevaDepartment of Biological Sciences, Carnegie Mellon University 4400 Fifth Avenue Pittsburgh PA 15213 USA.
Hironobu MurataCenter for Polymer-Based Protein Engineering, Carnegie Mellon University 5000 Forbes Avenue Pittsburgh PA 15213 USA.
Krzysztof MatyjaszewskiCenter for Polymer-Based Protein Engineering, Carnegie Mellon University 5000 Forbes Avenue Pittsburgh PA 15213 USA.
Alan J RussellDepartment of Biological Sciences, Carnegie Mellon University 4400 Fifth Avenue Pittsburgh PA 15213 USA.
Susanne BoyeCenter Macromolecular Structure Analysis, Leibniz-Institut für Polymerforschung Dresden e.V. Hohe Straße 6 Dresden 01069 Germany lederer@ipfdd.de alederer@sun.ac.za.ORCID https://orcid.org/0000-0003-1223-2434
Albena LedererCenter Macromolecular Structure Analysis, Leibniz-Institut für Polymerforschung Dresden e.V. Hohe Straße 6 Dresden 01069 Germany lederer@ipfdd.de alederer@sun.ac.za.ORCID https://orcid.org/0000-0002-1760-6426

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polymer-based protein engineering has enabled the synthesis of a variety of protein-polymer conjugates that are widely applicable in therapeutic, diagnostic and biotechnological industries. Accurate characterizations of physical-chemical properties, in particular, molar masses, sizes, composition and their dispersities are critical parameters that determine the functionality and conformation of protein-polymer conjugates and are important for creating reproducible manufacturing processes. Most of the current characterization techniques suffer from fundamental limitations and do not provide an accurate understanding of a sample's true nature. In this paper, we demonstrate the advantage of asymmetrical flow field-flow fractionation (AF4) coupled with multiple detectors for the characterization of a library of complex, zwitterionic and neutral protein-polymer conjugates. This method allows for determination of intrinsic physical properties of protein-polymer chimeras from a single, rapid measurement.

Identifiers

PMID34760170
PMCPMC8549772

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