CoChat
Sign Up
Cited by 109Collagen: Extraction and CharacterizationSilk-based biomaterials and applicationsConnective tissue disorders research

Three Decades of Research on Recombinant Collagens: Reinventing the Wheel or Developing New Biomedical Products?

Open access
Fertala, Andrzej·2020·Bioengineering
DOI 10.3390/bioengineering7040155PMC PMC7712652
Open this paper in CoChat — free accountOpen PDF

Abstract

Collagens provide the building blocks for diverse tissues and organs. Furthermore, these proteins act as signaling molecules that control cell behavior during organ development, growth, and repair. Their long half-life, mechanical strength, ability to assemble into fibrils and networks, biocompatibility, and abundance from readily available discarded animal tissues make collagens an attractive material in biomedicine, drug and food industries, and cosmetic products. About three decades ago, pioneering experiments led to recombinant human collagens' expression, thereby initiating studies on the potential use of these proteins as substitutes for the animal-derived collagens. Since then, scientists have utilized various systems to produce native-like recombinant collagens and their fragments. They also tested these collagens as materials to repair tissues, deliver drugs, and serve as therapeutics. Although many tests demonstrated that recombinant collagens perform as well as their native counterparts, the recombinant collagen technology has not yet been adopted by the biomedical, pharmaceutical, or food industry. This paper highlights recent technologies to produce and utilize recombinant collagens, and it contemplates their prospects and limitations.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/bioengineering7040155

Cites

159 of 159 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The ability of ECM peptides to trigger corresponding receptors on immune cells depends on the tertiary conformation of molecules.

    “The ability of ECM peptides to trigger corresponding receptors on the immune cells also depends on the tertiary conformation of molecules [114].”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [114]

    Section 2.4 says collagen receptor binding depends on structure: linear peptides can bind weakly and may fail to trigger cell responses, while some receptors require collagen fibrils. It lists the leukocyte-associated receptor LAIR-1, but does not establish this dependence for ECM peptides generally or specifically demonstrate responses in immune cells. No page number is available in our copy. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Interspecies variations between ECM components such as collagen, laminin, fibronectin, elastin, and growth factors are not extreme, making xenogeneic ECM plausible surrogates for their human-derived counterparts.

    “Interspecies variations between ECM components such as collagen, laminin, fibronectin, elastin, and growth factors are not extreme, making xenogeneic ECM plausible surrogates for their human-derived counterparts [114, 117–119].”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [114]

    Section 3.2 (page not available) says animal and human collagen triple-helical regions share significant similarities, which supports part of the claim. It also identifies substantial differences in their telopeptide regions. The paper does not establish that interspecies differences are small for laminin, fibronectin, elastin, or growth factors, or that xenogeneic ECM as a whole is a surrogate for human ECM. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 2

  1. [17]Royce P.M. Steinmann B. Connective Tissue and Its Heritable Disorders: Molecular, Genetic, and Medical Aspects 2nd ed. John Wiley & Sons Hoboken, NJ, USA 2002 1201
  2. [65]Brodsky B. Ramshaw J.A. Bioengineered collagens Subcell. Biochem. 2017 82 601 629 28101874

Cited by

Sorted by citations

Authors
Fertala, A.
Affiliations
Thomas Jefferson University (US)
Corresponding author
Fertala, Andrzej
ORCID
Fertala, Andrzej
Venue
Bioengineering
Publisher
MDPI AG
Published
2020-12-02
Volume
7
Issue
4
Pages
155
ISSN
2306-5354 (ISSN-L)
DOI
10.3390/bioengineering7040155
PMC
PMC7712652
OpenAlex
W3109266820
Cited by
109
References
159
Citations by year
2026: 18 · 2025: 30 · 2024: 24 · 2023: 16 · 2022: 13 · 2021: 8
FWCI
0.62
Type
journal article
Language
en
Open access
Licence
Locations
  • Bioengineering (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • The Medicine Forum (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
Keywords
recombinant collagen, recombinant human collagen, collagen fragments, collagen fibril assembly, tissue engineering, drug delivery, biocompatibility, recombinant protein expression systems, collagen-based biomaterials

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review