Evidence map›Paper›PMID 37275756›Full record

ArticleIranian journal of basic medical sciences2023

Amino acid-mPEGs: Promising excipients to stabilize human growth hormone against aggregation.

Somayeh Vakili, JamshidKhan Chamani, Zeinab Amiri-Tehranizadeh, Hossein Hosseinzadeh, Fatemeh Mosaffa, Seyed-Mola Khatami, Bahman Khameneh, Mohammad Reza Saberi

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In one paragraph

Article in Iranian journal of basic medical sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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 3 institutions in 1 country.

Somayeh VakiliDepartment of Medical Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
JamshidKhan ChamaniDepartment of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran.
Zeinab Amiri-TehranizadehDepartment of Medical Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
Hossein HosseinzadehDepartment of Pharmacodynamics and Toxicology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
Fatemeh MosaffaBiotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran.
Seyed-Mola KhatamiDepartment of Chemistry, Faculty of Samen Hojaj, Mashhad Branch, Technical and Vocational University (TVU), Tehran, Iran.
Bahman KhamenehDepartment of Pharmaceutical Control, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
Mohammad Reza SaberiDepartment of Medical Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
Mashhad University of Medical Sciences · IRIslamic Azad University, Mashhad · IRTechnical and Vocational University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Objectives: Today, the non-covalent PEGylation methods of protein pharmaceuticals attract more attention and possess several advantages over the covalent approach. In the present study, Amino Acid-mPEGs (aa-mPEGs) were synthesized, and the human Growth Hormone (hGH) stability profile was assessed in their presence and absence. Materials and Methods: aa-mPEGs were synthesized with different amino acids (Trp, Glu, Arg, Cys, and Leu) and molecular weights of polymers (2 and 5 KDa). The aa-mPEGs were analyzed with different methods. The physical and structural stabilities of hGH were analyzed by SEC and CD spectroscopy methods. Physical stability was assayed at different temperatures within certain intervals. Molecular dynamics (MD) simulation was used to realize the possible mode of interaction between protein and aa-mPEGs. The cell-based method was used to evaluate the cytotoxicity. Results: HNMR and FTIR spectroscopy indicated that aa-mPEGs were successfully synthesized. hGH as a control group is known to be stable at 4 Conclusion: This paper showed that aa-mPEGs are potent excipients in decreasing the aggregation of hGH. Glu-mPEG exhibited the best-stabilizing properties in a harsh environment among other aa-mPEGs.

Indexed as

Human growth hormoneNon-covalent PEGylationPhysical PEGylationProtein formulationStability

Identifiers

PMID37275756
PMCPMC10237159
OpenAlexW4379507985

What OpenQuestion holds

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Registered trials

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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.