Evidence map›Paper›PMID 38898654›Full record

ArticleBiophysical journal2024

Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin.

John J Correia, Walter F Stafford, Heidi Erlandsen, James L Cole, Sanduni H Premathilaka, Dragan Isailovic, John David Dignam

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

John J CorreiaDepartment of Cell & Molecular Biology, University of Miss Medical Center, Jackson, Mississippi. Electronic address: jcorreia@umc.edu.
Walter F StaffordDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts.
Heidi ErlandsenCenter for Open Research Resources and Equipment, University of Connecticut, Storrs, Connecticut.
James L ColeDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut.
Sanduni H PremathilakaDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio.
Dragan IsailovicDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio.
John David DignamDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Covalent labeling of therapeutic drugs and proteins with polyethylene glycol (PEGylation) is an important modification for improving stability, solubility, and half-life. PEGylation alters protein solution behavior through its impact on thermodynamic nonideality by increasing the excluded volume, and on hydrodynamic nonideality by increasing the frictional drag. To understand PEGylation's impact, we investigated the thermodynamic and hydrodynamic properties of a model system consisting of PEGylated human serum albumin derivatives using analytical ultracentrifugation (AUC) and dynamic light scattering (DLS). We constructed PEGylated human serum albumin derivatives of single, linear 5K, 10K, 20K, and 40K PEG chains and a single branched-chain PEG of 40K (2 × 20K). Sedimentation velocity (SV) experiments were analyzed using SEDANAL direct boundary fitting to extract ideal sedimentation coefficients s

Indexed as

Polyethylene GlycolsSerum Albumin, HumanHumansHydrodynamicsThermodynamicsUltracentrifugationPolyethylene GlycolsSerum Albumin, Human

Identifiers

PMID38898654
PMCPMC11365110

What OpenQuestion holds

Textmetadata
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.