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The most abundant protein in the human body is collagen. Collagen comes in various flavors but their
structures are based on the same protein chemistry. A single collagen molecule or tropocollagen is made up
of three polypeptide strands wound together in a helical manner. Multiple tropocollagens bind together to
form a microfibril. Microfibrils, in turn, align in parallel to form a larger bundle structure known as fibril. Many
fibrils form the collagen fiber. Collagen fibers are omnipresent in the body, indicating its functional importance.
Cells rely on collagen to attach to extracellular matrix (a complex mixture of non-living materials) to
organize themselves into tissues. In turn, each tissue depends on collagen for attachment to form organs.
Finally, collagen allows organs to unite to form a complex multi-organ organism. Collagen is like a biological
adhesive for its role in tissue and organ formations. Without this biological adhesive, all tissues and organs
would break down into a disorganized mass of cells. Conversely, if cells are removed from tissues and organs,
the resulting structural network is consisted mainly of collagen.
Collagen is widely used in the medical, cosmetic, and research fields. A popular source of collagen is
animal tissues. Because collagen in the body is completely bound up due to its intermolecular cross-linking,
cleaving these cross-links, or solubilizing the collagen is necessary. One method of collagen solubilization
utilizes proteases, enzymes that break the cross-links between collagen molecules. Collagen obtained through
solubilization is called atelocollagen. Collagen is known for its very low antigenicity (causing immune responses)
because most of the collagen molecule is composed of a G-X-Y amino acid sequence that differs little even
among different animal species. Greatest antigenicity observed in collagen is caused by telopeptides at each
end of the collagen molecule, which do not contain the G-X-Y sequence. Unfortunately, this method of
obtaining purified collagen has many drawbacks:
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Purification of atelocollagen is extremely time-consuming and costly
Purification makes the collagen molecules vulnerable to protease degradation
Purification exposes telopeptides
Cross-linking agents make collagen fibers stronger but they can lead to allergic side effects and are
potential carcinogens
Simply CANNOT reconstruct the collagen matrix with the same pore size and tensile strength
through artificial means as compared to what has been done by nature
Therefore, ACRO Biomedical Company, Ltd. (ABC) decided not to
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Purify collagen from animal tissues, thus
Worry about the presence of telopeptides
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Go through the time consuming and costly purification and re-polymerization processes
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Worry about the fast degradation of the traditionally purified collagen
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Use toxic chemicals for cross-linking
Instead, lipids, proteins, and cells from animal tissues will be removed using ACRO Biomedical exclusive
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supercritical CO2-based minimal manipulation process, leaving intact collagen scaffolds. Since telopeptides are
deeply buried in the intact scaffold structure, the
likelihood of immune reaction is extremely low.
Meanwhile, the pore size and tensile strength of the
scaffold are maintained, ideal for natural tissue
regeneration.
ACRO Biomedical offers biomedical grade ABCcolla®
Collagen (150 to 300 kDa) for various medical and
research applications.