Tier 4 — mechanistic

Current insights into collagen type I

Ruth Naomi, Pauzi Muhd Ridzuan, Hasnah Bahari
Polymers 2021 13(16):2642

Bibliography

PubMed
PMID 34451183
PubMed Central
PMC8399689
Funding
Funding statement (verbatim): "This study was funded by Research Management Centre (RMC) UPM for APC payment. The funder does not have any contribution and decision to publish or preparation of the manuscript."
Competing interests
Competing interests statement (verbatim): "The authors declare no conflict of interest." All three authors affiliated with Universiti Putra Malaysia (Department of Human Anatomy) and Estika Research Centre (Kuala Terengganu, Malaysia) — academic institutions with no commercial industry ties surfaced. Funding limited to article processing charge only, with explicit statement of no funder involvement in manuscript preparation. Clean commercial-independence profile.

Study snapshot

DesignComprehensive narrative review covering structure, availability, native synthesis, extraction methods, physicochemical characteristics, applications across pharmaceutical, cosmeceutical, regenerative medicine, and clinical fields
ModelNot applicable — review paper. Covers evidence from prior 5 years primarily.
SampleNot applicable
InterventionNot applicable
DurationReview methodology; covers literature primarily from the prior 5 years to the 2021 publication date
EndpointsComprehensive coverage of: molecular structure of collagen type I; sources (marine, bovine, porcine, chicken, egg); native biosynthesis pathway; current extraction and processing methods; physicochemical properties; applications across pharmaceutical, cosmeceutical, regenerative medicine, and clinical fields; biomarker overview

What the study showed, in plain terms

Collagen is the most abundant protein in the human body — it makes up roughly a third of all the protein we contain. But collagen isn't a single molecule. There are 28 different types identified so far, each doing slightly different jobs in different tissues. Type I collagen is the dominant form, accounting for around 90 percent of the collagen in skin, bones, tendons, teeth, corneas, and the outer coverings of organs. Almost every clinical trial of oral collagen supplements uses type I collagen extracted from cow hide, pig skin, fish scales, chicken bone, or egg membrane.

This 2021 review from researchers at Universiti Putra Malaysia is a technical reference document — the kind of paper the pillar cites to establish what collagen actually is at the molecular level before discussing what it does. The authors comprehensively cover the triple-helix molecular structure, the biology of how the body makes collagen from scratch, all the current commercial extraction methods used to turn animal hides, bones, and scales into supplement powder, the physical and chemical properties that make type I collagen so useful in medicine, and the wide range of applications spanning wound healing, drug delivery, 3D-printed tissue scaffolds, cosmetics, and dietary supplements.

Unlike the clinical trial papers in this Data Center, this review does not report an intervention or an outcome. Its value is as the foundational biology reference that gives every other cited paper its context. When the pillar states that collagen makes up 90 percent of the protein in human skin, or when the "what is hydrolysed collagen" article explains that hydrolysis breaks the intact triple helix into smaller peptides, this is the paper that anchors those factual claims. Independent academic authorship and government-funded article processing charge make it the cleanest available reference for these foundational statements.

Key findings

  • Collagen type I is the most abundant protein in the human body, accounting for approximately 90% of total body protein.
  • Found predominantly in skin, bones, tendons, capsule of organs, cornea, and fascia — absent from cartilaginous tissues (which are dominated by type II collagen).
  • 28 different types of collagen have been identified to date. Type I is the fibril-forming reference type used across most tissue engineering and supplementation research.
  • Native molecular structure: triple-helix composed of α1(I) and α2(I) polypeptide chains encoded by COL1A1 and COL1A2 genes.
  • Collagen type I can exist as homotrimer (three α1 chains) or heterotrimer (two α1 + one α2). Heterotrimers dominate in normal tissue; homotrimers appear in fibrotic lesions, fetal tissue, and some tumours.
  • Approximately 1,000+ amino acids per collagen molecule, forming a fibril up to 300 nm long and 1–5 nm wide.
  • Commercial sources: marine (fish skin/scales), bovine (cow hide), porcine (pig skin), chicken (bone/cartilage), egg (membrane) — each with distinct amino acid composition and processing profiles.
  • Review comprehensively covers extraction methods (acid, enzymatic, alkaline), physicochemical characterisation, and applications spanning pharmaceutical, cosmeceutical, regenerative medicine, and clinical fields.

What this study can and cannot tell us

  • Narrative review, not a systematic review — no PRISMA-compliant search protocol or formal inclusion criteria applied.
  • Explicit scope limited to the prior 5 years — foundational literature older than 2016 is under-represented.
  • Applications section covers many domains at moderate depth — for detailed clinical evidence on any specific application (skin, joint, bone), other dedicated reviews are stronger.
  • Does not directly address the oral supplementation clinical question — this is a biology/chemistry review, not a supplementation review.
  • Some sections are dense with molecular-level detail that requires biochemistry background to interpret — practical accessibility for lay readers is limited.
  • Published in Polymers (an MDPI journal focused on polymer science) rather than a clinical journal — indexing and clinical audience reach differ accordingly.
Reviewed by , Medical Advisory Board · Last verified against PubMed on 30 August 2026