Origin |
Animals/humans |
Col from bones/skin |
Precursor |
Fibroblast |
Col type I |
Physical characteristics |
Elastic, tough and versatile structural protein |
Smooth and gel like substances |
Number of Amino acids |
Approximately 1050 |
Less than 20 |
Structure of peptide |
Triple helix of polypeptide chain |
Small peptides |
Types |
Fibril-forming and nonfibril forming |
A and B |
Aromatic radicals |
Present |
Absent |
Solubility |
NaCI solution/dilute acid |
H2O |
Mechanical strength |
Poor |
Poor |
Antigenic response |
Possible, in case of crosslinking/integration with antibacterial agent |
Impossible, Because of its hydrophilicity nature. |
Digestion |
Difficult |
Easy |
Protease |
Resistant |
Susceptible |
Gelling properties |
No |
Yes |
In vitro degradation |
Serine protease, pepsin-cleaving enzyme, gelatinease and collagenase |
Collagenase |
In vivo degradation |
Endopeptidase |
MMP-2 and MMP-9 |
Disease transmission |
Xenozoonoses if the Col is impure |
Not encountered |
Usage |
Burns, hemostasis, tissue defects, regeneration of nerves, wound dressings, augmentation of soft tissue, artificial dermis skin replacement |
Adhesive of soft tissues, artificial skin, regeneration of nerves, wound dressings |