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. 2022 Jun 14;15:100322. doi: 10.1016/j.mtbio.2022.100322

Table 1.

Fibril-forming properties of different types of collagen.

Acid-soluble Enzyme-treated Alkali-treated
Molecular structure intact telopeptides cleaved deamidized asparagine and glutamine amino acids and telopeptides cleaved
Gelation Possible at low concentration of collagen Possible at high concentration of collagen at acidic pH with the appearance of non-banded filaments
Ability to form native banded fibrils Yes Yes, but less well organized No
Adhesion of cells to substrata from this type of collagen Good Good Good
Advantages Ability to form native banded well-ordered collagen fibrils at optimal conditions
Ability to form stable collagen gels at very low concentration of collagen
Ability to form collagen gels with a high concentration of collagen
Obliquely banded fibrils, FLS and SLS can be obtained
Suitable for the production of non-fibrous collagen materials (films, sponge, etc.)