Evidence map›Paper›PMID 33641212›Full record

ArticleClinical and translational science2021

Estimating peptide half-life in serum from tunable, sequence-related physicochemical properties.

Marco Cavaco, Javier Valle, Isabel Flores, David Andreu, Miguel A R B Castanho

Open access · goldAbstract read
In one paragraph

Article in Clinical and translational science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Virtual screening and experimental validation of a METTL3-targeting peptide withJournal of enzyme inhibition and medicinal chemistry · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. AI Designed Conformation Locking Peptides Target STING to Restore Diabetic Wound Healing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. New Trends in Brain Shuttle Peptides.Molecular pharmaceutics · 2025
    Review
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 2 countries.

Marco CavacoInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal.
Javier ValleProteomics and Protein Chemistry Unit, Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona, Spain.
Isabel FloresInstituto das Políticas Públicas e Sociais do ISCTE, Lisboa, Portugal.
David AndreuProteomics and Protein Chemistry Unit, Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona, Spain.
Miguel A R B CastanhoInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal.
Pompeu Fabra University · ESIscte – Instituto Universitário de Lisboa · PTUniversity of Lisbon · PT

Funding

European Union H2020-MSCA-RISE-2014 program 828774"La Caixa" Banking Foundation HR17-00409Portuguese Fundação para a Ciência e a Tecnologia PD/BD/128281/2017Portuguese Fundação para a Ciência e a Tecnologia PTDC/BBB-NAN/1578/2014Portuguese Fundação para a Ciência e a Tecnologia PTDC/BIA-VIR/29495/2017Portuguese Fundação para a Ciência e a Tecnologia PTDC/QUI-NUC/30147/2017Portuguese Fundação para a Ciência e a Tecnologia UID/Multi/04349/2019Spanish Ministry of Economy and Innovation AGL2014-52395-C2-2-RSpanish Ministry of Economy and Innovation AGL2017-84097-C2-2-R
6 · The paper itself

Abstract

Proteolytic instability is a critical limitation for peptide-based products. Although significant efforts are devoted to stabilize sequences against proteases/peptidases in plasma/serum, such approaches tend to be rather empirical, unspecific, time-consuming, and frequently not cost-effective. A more rational and potentially rewarding alternative is to identify the chemical grounds of susceptibility to enzymatic degradation of peptides so that proteolytic resistance can be tuned by manipulation of key chemical properties. In this regard, we conducted a meta-analysis of literature published over the last decade reporting experimental data on the lifetimes of peptides exposed to proteolytic conditions. Our initial database contained 579 entries and was curated with regard to amino acid sequence, chemical modification, terminal half-life (t

Indexed as

Amino Acid SequenceChemistry, PharmaceuticalComputational ChemistryHalf-LifeHumansModels, BiologicalModels, ChemicalMolecular WeightPeptidesProtein StabilityProteolysisPeptides

Identifiers

PMID33641212
PMCPMC8301568
OpenAlexW3134841439

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.