Evidence map›Paper›PMID 34758508›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Control over Multiple Nano- and Secondary Structures in Peptide Self-Assembly.

Goutam Ghosh, Ranajit Barman, Anurag Mukherjee, Uttam Ghosh, Suhrit Ghosh, Gustavo Fernández

Abstract 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 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
–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

21 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Induction and Stabilization of Peptide Alpha-Helices on Silica Nanoparticles.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Self-Assembling Short Peptide Carriers for Gene Delivery.International journal of molecular sciences · 2026
    Review
  7. Article
  8. Article
  9. Antioxidant Peptide-Based Nanocarriers for Delivering Wound Healing Agents.Tissue engineering and regenerative medicine · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Control over Multiple Nano- and Secondary Structures in Peptide Self-Assembly.Angewandte Chemie (International ed. in English) · 2022
    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

6 authors.

Goutam GhoshOrganisch-Chemisches Institut, Westfälische Wilhelms-Universität Münster, Correnstrasse 36, 48149, Münster, Germany.ORCID 0000-0002-3823-5265
Ranajit BarmanSchool of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation Science, 2A and 2B Raja S. C. Mullick Road, Kolkata, India.
Anurag MukherjeeSchool of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation Science, 2A and 2B Raja S. C. Mullick Road, Kolkata, India.ORCID 0000-0002-4242-3509
Uttam GhoshDepartment of Organic Chemistry, Indian Institute of Science, Bengaluru, 560012, Karnataka, India.
Suhrit GhoshSchool of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation Science, 2A and 2B Raja S. C. Mullick Road, Kolkata, India.ORCID 0000-0003-4199-4382
Gustavo FernándezOrganisch-Chemisches Institut, Westfälische Wilhelms-Universität Münster, Correnstrasse 36, 48149, Münster, Germany.ORCID 0000-0001-6155-8671

Funding

H2020 European Research Council ERC-StG-2016 SUPRACOP-715923
6 · The paper itself

Abstract

Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP-1), which follows diverse self-assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP-1 forms twisted β-sheet secondary structures and nanofibers at pH 7.4, which transform into fractal-like structures with strong β-sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted β-sheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two self-assembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted β-sheet structures and corresponding nanofibers transform into 2D sheets with well-defined β-sheet domains, the nanoparticles with random coil structures convert into short nanorods with α-helix conformations. Notably, PEP-1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio-applications.

Indexed as

PeptidesProtein Structure, SecondaryAnti-Bacterial AgentsHumansHydrogen-Ion ConcentrationMicrobial Sensitivity TestsNanofibersNanostructuresAnti-Bacterial AgentsPeptidesamphiphilic systemsnanostructurespeptidessecondary structuresself-assembly

Identifiers

PMID34758508
PMCPMC9300061

What OpenQuestion holds

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LicenceCC BY-NC
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.