Evidence map›Paper›PMID 38090079›Full record

ReviewRSC advances2023

Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.

Mahdie Rahban, Faizan Ahmad, Mieczyslaw A Piatyszek, Thomas Haertlé, Luciano Saso, Ali Akbar Saboury

Abstract readReview
In one paragraph

Review in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Recombinant Protein Drugs: A 2025 Update.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  9. Therapeutic peptides and proteins: Status and developments in drug delivery.Journal of controlled release : official journal of the Controlled Release Society · 2026
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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.

Mahdie RahbanNeuroscience Research Center, Institute of Neuropharmacology, Kerman University of Medical Sciences Kerman Iran mrohban@ut.ac.ir.ORCID https://orcid.org/0000-0003-2924-9101
Faizan AhmadDepartment of Biochemistry, School of Chemical & Life Sciences, Jamia Hamdard New Delhi-110062 India faizanahmad@jamiahamdard.ac.in.
Mieczyslaw A PiatyszekBiotechnology Consultant Gainesville FL USA piatyszekm@gmail.com.ORCID https://orcid.org/0000-0003-0502-3239
Thomas HaertléNational Institute of Agronomic Research Nantes France tom@haertle.fr.ORCID https://orcid.org/0000-0002-1696-2269
Luciano SasoDepartment of Physiology and Pharmacology "Vittorio Erspamer", Sapienza University Rome Italy luciano.saso@uniroma1.it.
Ali Akbar SabouryInstitute of Biochemistry and Biophysics, University of Tehran Tehran 1417614335 Iran saboury@ut.ac.ir +9821 66404680 +9821 66956984.ORCID https://orcid.org/0000-0003-0604-9465

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-based therapeutics have revolutionized the pharmaceutical industry and become vital components in the development of future therapeutics. They offer several advantages over traditional small molecule drugs, including high affinity, potency and specificity, while demonstrating low toxicity and minimal adverse effects. However, the development and manufacturing processes of protein-based therapeutics presents challenges related to protein folding, purification, stability and immunogenicity that should be addressed. These proteins, like other biological molecules, are prone to chemical and physical instabilities. The stability of protein-based drugs throughout the entire manufacturing, storage and delivery process is essential. The occurrence of structural instability resulting from misfolding, unfolding, and modifications, as well as aggregation, poses a significant risk to the efficacy of these drugs, overshadowing their promising attributes. Gaining insight into structural alterations caused by aggregation and their impact on immunogenicity is vital for the advancement and refinement of protein therapeutics. Hence, in this review, we have discussed some features of protein aggregation during production, formulation and storage as well as stabilization strategies in protein engineering and computational methods to prevent aggregation.

Identifiers

PMID38090079
PMCPMC10711991

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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.