Evidence map›Paper›PMID 32939884›Full record

ArticleProtein science : a publication of the Protein Society2020

Self-assembling peptides: From a discovery in a yeast protein to diverse uses and beyond.

Shuguang Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-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, 44 citations in OpenAlex.

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  3. Modulating Peptide Self-Assembly via Triblock Chiral Patterning.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
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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

1 author at 1 institution in 1 country.

Shuguang ZhangLaboratory of Molecular Architecture, Media Lab, Massachusetts Institute of Technology, 77 Massachusetts Avenue E15-391, Cambridge, Massachusetts, 02139-4306, USA.ORCID 0000-0002-3856-3752
Massachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Well-defined nanofiber scaffold hydrogels made of self-assembling peptides have found their way into various 3D tissue culture and clinical products. I reflect initial puzzlement of the unexpected discovery, gradual understanding of how these peptides undergo self-assembly, to eventually translating designer biological scaffolds into commercial products. Peptides are ubiquitous in nature and useful in many fields. They are found as hormones, pheromones, antibacterial, and antifungal agents in innate immunity systems, toxins, as well anti-inset pesticides. However, the concept of peptides as materials was not recognized until 1990 when a self-assembling peptide as a repeating segment in a yeast protein was serendipitously discovered. The peptide materials have bona fide materials properties and are made from simple amino acids with well-ordered nanostructures under physiological conditions. Some current applications include: (a) Real 3D tissue cell cultures of diverse tissue cells and various stem cells; (b) reparative and regenerative medicine as well as tissue engineering; (c) 3D tissue printing; (d) sustained releases of small molecules, growth factors and monoclonal antibodies; and (e) accelerated wound healing of skin and diabetic ulcers as well as instant hemostasis in surgery. Self-assembling peptide nanobiotechnology will likely continue to expand in many directions in the coming years. I will also briefly introduce my current research using a simple QTY code for membrane protein design. I am greatly honored and humbled to be invited to contribute an Award Winner Recollection of the 2020 Emil Thomas Kaiser Award from the Protein Society.

Indexed as

NanostructuresPeptidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptidesSaccharomyces cerevisiae Proteins3D tissue cell culturesdesigner peptidesEAK16 & RADA16membrane protein designnanofiber scaffold hydrogelQTY coderegenerative medicinesustained molecular releasetissue repair

Identifiers

PMID32939884
PMCPMC7586918
OpenAlexW3087420131

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.