Evidence map›Paper›PMID 35922375›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Atomic-Scale View of Protein-PEG Interactions that Redirect the Thermal Unfolding Pathway of PEGylated Human Galectin-3.

Amanda Pritzlaff, Guillaume Ferré, Emma Mulry, Ling Lin, Niloofar Gopal Pour, Daniel A Savin, Michael E Harris, Matthew T Eddy

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

8 authors at 1 institution in 1 country.

Amanda PritzlaffDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0002-7920-2021
Guillaume FerréDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0001-9519-0676
Emma MulryDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Ling LinDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0002-6446-1944
Niloofar Gopal PourDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Daniel A SavinDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0002-9235-517X
Michael E HarrisDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0001-8977-4392
Matthew T EddyDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0002-3349-6212
University of Florida · US

Funding

R35 Supplement - Equipment SupplementR35GM138291 · NIGMS · UNIVERSITY OF FLORIDA · PI Matthew Thomas Eddy · 2020 to 2026
$2.5M
Specificity in Substrate Recognition and Catalysis by RNA Processing EnzymesR35GM127100 · NIGMS · UNIVERSITY OF FLORIDA · PI HARRIS, MICHAEL E. · 2018 to 2022
$1.6M
Chemistry-Biology Interface Training Program at the University of FloridaT32GM136583 · NIGMS · UNIVERSITY OF FLORIDA · PI Chenglong Li · 2020 to 2026
$1.1M
Acquisition of a Q Exactive HF Hybrid Quadrupole-OrbitrapS10OD021758 · OD · UNIVERSITY OF FLORIDA · PI BASSO, KARI B · 2017 to 2017
$600k
NIGMS NIH HHS R35 GM127100NIGMS NIH HHS R35 GM138291NIGMS NIH HHS T32 GM136583NIH HHS S10 OD021758
6 · The paper itself

Abstract

PEGylation is a promising approach to address the central challenge of applying biologics, i.e., lack of protein stability in the demanding environment of the human body. Wider application is hindered by lack of atomic level understanding of protein-PEG interactions, preventing design of conjugates with predicted properties. We deployed an integrative structural and biophysical approach to address this critical challenge with the PEGylated carbohydrate recognition domain of human galectin-3 (Gal3C), a lectin essential for cell adhesion and potential biologic. PEGylation dramatically increased Gal3C thermal stability, forming a stable intermediate and redirecting its unfolding pathway. Structural details revealed by NMR pointed to a potential role of PEG localization facilitated by charged residues. Replacing these residues subtly altered the protein-PEG interface and thermal unfolding behavior, providing insight into rationally designing conjugates while preserving PEGylation benefits.

Indexed as

Biological ProductsGalectin 3CarbohydratesHumansPolyethylene GlycolsProtein StabilityBiological ProductsCarbohydratesGalectin 3Polyethylene GlycolsBiologicsNMR SpectroscopyPEGylated ProteinsProtein EngineeringProtein-Polymer Conjugate

Identifiers

PMID35922375
PMCPMC9529833
OpenAlexW4289711198

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.