9007-34-5 Usage
Description
Collagen is a naturally occurring protein that is the main component of the extracellular matrix and is found in various connective tissues such as skin, bone, tendon, and ligaments. It is composed of repeating triplet amino acids glycine, proline, and hydroxyproline, and has a unique triple helix structure. Collagen is biocompatible, biodegradable, and has low immunogenicity, making it a valuable resource in various industries.
Uses
Used in Healthcare Industry:
Collagen is used as scaffolds, skin, and bones in tissue engineering. It has good biocompatibility and biodegradable security, making it suitable for applications such as vascular membranes, ligaments, and heart valves. Collagen also has a unique skin repair function, making it useful for skin transplants after modification. It plays a role in anchoring and supporting cells, providing the appropriate microenvironment for cell proliferation and growth, and supplying nutrients. Collagen is used for burns and trauma repair, treatment and care, reducing and alleviating the degree of burns. Collagen biological dressings have advantages such as simple preparation methods, good adhesion, and suitability for the formation of granulation tissue and epithelial cells.
Collagen protein is also used to treat ophthalmic diseases, promoting cell growth and repair of corneal epithelial cell damage. It can be dissolved in tears and has the ability to introduce epithelial cells into the defect area. Its degraded products can be used by new cells for new collagen synthesis, making it widely applied in the treatment of eye diseases. Collagen can also be used as a carrier for ocular administration, increasing drug concentration, prolonging drug action time, and reducing systemic toxicity.
In clinical medicine, collagen is used for cosmetic and orthopedic treatments, periodontal disease treatment, hard tissue repair, nerve repair and regeneration, as wrapping materials for periodontal nerve repair, artificial organs, pacemakers, and filling materials for human organs.
Used in Cosmetics:
Collagen can be extracted from animal skin and contains proteoglycans like hyaluronic acid and chondroitin sulfate, which are important for maintaining skin moisture. It also prevents the conversion of tyrosine into melanin in the skin. Collagen promotes the proliferation and repair of epithelial cells, replenishes amino acids and nutrients, improves the living environment of skin cells, promotes metabolism and circulation, fills and repairs damaged and aging skin, and has good compatibility, affinity, and permeability with the skin. It is widely used in cosmetics such as masks, eye creams, and skin creams.
Used in Food Industry:
Collagen peptides can be taken as a functional food, such as chewable tablets, protein powders, or enteral nutrition agents for athletes. Foods rich in collagen can delay aging, strengthen gluten and bones, enhance physical fitness, and have health effects like weight and blood pressure reduction and calcium replenishment. Hydrolyzed collagen can be used as a modifier for meat products, improving connective tissue, increasing protein content, and enhancing taste and nutrition. Collagen hydrolysis products can be used as thickening agents in frozen foods, jelly, sour cheese, ham, canned food, and bread. Collagen can also be used as membrane materials for solidified food and labels for meat, as well as a food adhesive for synthesizing film and a protective layer for food like meat and fish, which has antioxidant activity and maintains the bright color of meat.
Used in Other Fields:
Collagen has applications in various other fields, such as being a protein resource for animal feed from residual waste in the tanning process, improving textile properties after denaturation treatment for use in the textile industry, and being applied in light industry such as paper, leather, and daily chemical industries. With ongoing research and development, collagen is expected to have even broader applications in the future.
Other Uses:
Collagen is also used as surgical suture fibers, a substrate for measuring collagen, for collagenase binding, inhibiting carcinogenesis, and as a substrate for cell adhesion in tissue culture, gel formation, platelet aggregation, and as a cell culture substratum and attachment factor for primary cultures of epithelioid cells.
Structure properties
In molecular structure, collagen is composed of parallel linear chains, each linear chain consists of three twisted left-handed α-peptide chains which are closely connected by inter-chain interactions and be integrated to form a strong right-handed triple helix (triple-helix) structure. Each α-peptide chain is made up of more than 300 Gly-X-Y tandem repeat with other small segments of different structure connecting the two termini. Amino acid residues in collagen all belong to α-amino acid, wherein X, Y is any amino acid residue other than Gly, but usually for X: Pro; for Y is typically hydroxyproline (Hyp) which is not coded by DNA base. Hydroxyproline is formed by the action of a specific enzyme---proline-4-hydroxylase (prolyl-4-hydroxylase, P4H) on the proline after the formation of primary protein structure. Hydroxy group of hydroxyproline play an important role on stabilizing the helical structure of collagen via the hydrogen bonds. In addition, collagen also contains a certain amount of hydroxylysine (Hyl), which has a similar effect as Hyp. Because the side chains of Pro and Hyp are annular, the bonds between their α-carbon and the amide nitrogen cannot be rotated (The angle is generally fixed at about-60 °). Thereby the high content of these amino acid residues of boosts the formation of α-chain helical structure and further stabilize it. In the Triple-helix structure, GIy group is located in the center of the spiral, and the other amino acids which have a side chain are located outside of the spiral. The helix pitch of right-handed triple helix is 8.55 nm and its radius is 1.5nm. Every lap of each peptide chain contains 30 residues; and the length of every left-handed helical peptide chain is 0.952 nm. Each circle containing about 3.3 residues with the distance between axially adjacent amino acid residues being 0.286nm. Since the triple helix structure is a dislocation structure, the Gly residues come from three peptide chains piled up along the central axis of the helix. In the three-dimensional space, the Gly of chain is adjacent to the X and Y residues of the other two strands, respectively. The Gly in china A is close to the X residue of chain C and the Y residue in chain B. Therefore, the N-H of each Gly residue forms hydrogen bonds with CO of the adjacent X residues. Because hydroxy Hyp residues are also involved in the formation of hydrogen bonds between the chains, the triple helix structure is further stabilized and enhanced. Studies have shown that the presence of divalent iron ions at the N-terminal of collagen polypeptide can further improve the stability of the triple helical structure. In addition, the circular dichroism spectra reveal that polyhydroxy compounds such as sugar alcohols can polymerize with collagens. Molecular mechanics calculations further showed that the polymerization usually occurs in the position where X is Ser of collagen triplets. However, the stability of collagen will be weakened by the increased carbon atoms in such compounds.
Figure 2. The 3D structure of collagen
Physical and chemical property
Collagen protein is an amphoteric electrolyte depends on two factors, first, each of the collagen peptide chains having many acidic or basic side groups; Secondly, each of the collagen has α-carboxyl groups and α-amino groups in its two termini. These groups have the ability to accept or give a proton. The dissociable groups can yield either positive or negative charge in particular pH range. In other words, different collagens become ions with many positive charge or negative charge with different medium pH. PKI of the side chain of collagen peptide is slightly different from the PKI value of its amino acid side groups which is due to the influence of neighboring charge in the protein molecule. The isoelectric point of collagen (cowhide) is 7.5 to 7.8, exhibiting a slightly alkaline because the basic amino acid peptide chains of collagen are a little more than an acidic amino acid. As a polymer compound, collagen has colloidal properties and certain viscosity in an aqueous solution with the viscosity being lowest at the isoelectric point. The lower the temperature is, the greater the viscosity becomes.
The above information is edited by the lookchem of Dai Xiongfeng.
Biological properties
1. Low immunogenicity
As medical biomaterials, the most important feature of collagen is its low immunogenicity. There are three types of antigen molecules of collagen; the first category is the collagen telopeptide of the non-helical peptide chains; the second is the conformation of the triple helix of collagen, and the third category is the amino acid sequence of a-helix region; wherein the second kind of antigen is only presented in natural collagen molecule; the third kind of antigen only exists in denatured collagen; the first class I antigens factor are presented in both native and denatured collagen.
2. Biocompatibility
Good biocompatibility refers to the well interaction between collagen and host cells and tissues. Whether as the backbone of the new organization before being absorbed, or being assimilated into the host to become part of it, the collagen always has good interaction with the matrix surrounding them which exhibits the coordination of interaction with each other. Moreover, it will become the part of the integral of normal physiological function of cells and tissues.
3. Biodegradability
Collagen can be degraded by specific protease. That means it is biodegradable. Because collagen has a tightening and stable helical structure, the vast majority of protease can only cleave its side chains. Only with specific proteases under certain conditions can the peptide bonds of collagen be broken. Once the collagen peptide bonds were broken, its helical structure is destroyed immediately with the broken collagen polypeptide being totally degraded by protease.
Synthetic method
Use bovine tendon as the raw materials. Extract it with disodium hydrogen phosphate solution and KCl solution. Wash the residue, dehydrate and dry to obtain the finished product.
Biochem/physiol Actions
Collagen is essential for the mechanical integrity of tendons and bone. Rat tail tendon collagen is used in tissue engineering especially in the generation of 3-D scaffolds based gels. It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.
Check Digit Verification of cas no
The CAS Registry Mumber 9007-34-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,0 and 7 respectively; the second part has 2 digits, 3 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 9007-34:
(6*9)+(5*0)+(4*0)+(3*7)+(2*3)+(1*4)=85
85 % 10 = 5
So 9007-34-5 is a valid CAS Registry Number.
