Evidence map›Paper›PMID 32806033›Full record

ArticleACS nano2020

Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture.

Moumita Ghosh, Santu Bera, Sarah Schiffmann, Linda J W Shimon, Lihi Adler-Abramovich

Open access · hybridAbstract read
In one paragraph

Article in ACS nano, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Assessment of Bovine Collagen Manufactured via Cellular Agriculture.ACS biomaterials science & engineering · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Peptide-Based Hydrogels and Nanogels for Delivery of Doxorubicin.International journal of nanomedicine · 2021
    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 2 institutions in 1 country.

Moumita GhoshDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel.ORCID 0000-0002-8049-7330
Santu BeraDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel.ORCID 0000-0002-4830-552X
Sarah SchiffmannDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel.
Linda J W ShimonDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0002-7861-9247
Lihi Adler-AbramovichDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel.ORCID 0000-0003-3433-0625
Tel Aviv University · ILWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen, the most abundant protein in mammals, possesses notable cohesion and elasticity properties and efficiently induces tissue regeneration. The Gly-Pro-Hyp canonical tripeptide repeating unit of the collagen superhelix has been well-characterized. However, to date, the shortest tripeptide repeat demonstrated to attain a helical conformation contained 3-10 peptide repeats. Here, taking a minimalistic approach, we studied a single repeating unit of collagen in its protected form, Fmoc-Gly-Pro-Hyp. The peptide formed single crystals displaying left-handed polyproline II superhelical packing, as in the native collagen single strand. The crystalline assemblies also display head-to-tail H-bond interactions and an "aromatic zipper" arrangement at the molecular interface. The coassembly of this tripeptide, with Fmoc-Phe-Phe, a well-studied dipeptide hydrogelator, produced twisted helical fibrils with a polyproline II conformation and improved hydrogel mechanical rigidity. The design of these peptides illustrates the possibility to assemble superhelical nanostructures from minimal collagen-inspired peptides with their potential use as functional motifs to introduce a polyproline II conformation into hybrid hydrogel assemblies.

Indexed as

HydrogelsPeptidesAmino Acid SequenceAnimalsCollagenProtein ConformationCollagenHydrogelsPeptidespolyprolinecoassemblycollagen-inspiredhydrogelpolyproline II helixsingle crystal

Identifiers

PMID32806033
PMCPMC7450664
OpenAlexW3047480757

What OpenQuestion holds

Textmetadata
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.