ArticlePharmaceutical research2011
Multivalent and flexible PEG-nitrilotriacetic acid derivatives for non-covalent protein pegylation.
Article in Pharmaceutical research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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.
Who cites it
6 citing papers in PubMed, 34 citations in OpenAlex.
- Traceless linkers used for reversible protein-polymer conjugations.Chemical science · 2026Review
- Protein-polyelectrolyte complexation: effects of sterically repulsive groups, macromolecular architecture and hierarchical assembly.Soft matter · 2025Article
- From Synthesis to Characterization of Site-Selective PEGylated Proteins.Frontiers in pharmacology · 2019Review
- Facile Method of Protein PEGylation by a Mono-Ion Complex.ACS omega · 2017Article
- Nano-Armoring of Enzymes: Rational Design of Polymer-Wrapped Enzymes.Methods in enzymology · 2017Article
- Mix to validate: a facile, reversible PEGylation for fast screening of potential therapeutic proteins in vivo.Angewandte Chemie (International ed. in English) · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeA new approach for non-covalent protein PEGylation is translated from immobilized metal ion affinity chromatography, and based on metal coordination bonds between a chelating agent linked to PEG, nitrilotriacetic acid (NTA), and the ring nitrogen of histidines in a protein.
methodsPEG-NTA conjugates were synthesized differing in the number of NTA units and in the polymer structure. Three derivatives were investigated in association experiments with five model proteins. The most promising complex, PEG8-(NTA)(8)-Cu(2+)-G-CSF (granulocyte colony stimulating factor), was thoroughly characterized and the pharmacokinetic profile was evaluated in rats.
resultsThe experiments demonstrated that only PEG8-(NTA)(8), bearing eight NTA molecules on flexible PEG arms, associated strongly with those proteins having several histidines. The protein secondary structure was not affected in the complex. PEG8-(NTA)(8)-Cu(2+)-G-CSF showed a K (D) of 4.7 nM, as determined by surface plasmon resonance, but the association was not stable in vivo.
conclusionsPEG8-(NTA)(8) is the first derivative able to associate with native proteins and form soluble complexes with a nanomolar K (D). The study highlights the need of a multivalent and flexible coordination and encourages further investigations to increase the stability of PEG8-(NTA)(8) complexes in vivo either through the use of protein mutants or His-tag proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.