29 Questions
What is a common issue associated with hydrogels mentioned in the text?
Mechanical instability
How are fibrin hydrogels formed according to the text?
Enzymatic polymerization
What is the role of Metalloproteinases (MMPs) mentioned in the text?
Breaking down proteins
Which substances are used to control the rate of degradation in tissue engineering according to the text?
Plasmin and aprotinin
Why are Aprotinin and Tranexamic acid used in tissue engineering as mentioned in the text?
To control the rate of degradation by inhibiting plasmin
What is a key property of fibrin hydrogels that makes them desirable for tissue engineering according to the text?
Capability to promote angiogenesis
What determines the biophysical properties of gelatin gels?
Crosslinking
At what temperature does a reverse coil to triple helix transition occur in gelatin gels?
30°C
Why are chemical gels with glutaraldehyde preferred over natural methods?
They are inexpensive and easily accessible
How does pH affect gelatin gel strength in solution?
Decreases gel strength
Why do physical gelatin gels require crosslinkers for stability?
To prevent the gel from falling apart easily
What factor shows the most response in terms of gelation in gelatin gels?
$pH 5.0$
What is gelatin?
A form of irreversibly hydrolyzed collagen
Which process is used to produce gelatin?
Hydrolysis using heat and enzymes
What gives gelatin its thermoresponsive properties?
Random super coil formation upon hydrolysis
Why is gelatin considered biocompatible?
It does not induce toxicity and is less antigenic
What makes gelatin highly soluble compared to other ECM proteins?
Abundance of a specific amino acid sequence
Why is intact protein not necessary for gelatin in tissue engineering applications?
Only certain sections of the protein sequence are vital for cell attachment
What is the cleavage site on the α chain?
Gly-Pro-Arg
Why is the removal of the 'A' peptide cleavage strictly required for fibrin polymerization?
To improve the efficiency of polymerization
What interaction links the center of a fibrin assembly with the ends of two other fibrin assemblies?
Knob-hole binding
What is the function of thrombin in fibrin polymerization?
To remove fibrinopeptides
What do knob-hole interactions lead to in fibrin polymerization?
Formation of oligomers
What covers the knobs that are complementary to holes in fibrin polymerization?
/brinopeptides
What are the major disadvantages of using a fibrin-based scaffold for tissue engineering purposes?
Rapid degradation before proper tissue formation, squishing during sheet formation, and shrinkage of the gel
Which method can help reduce the rapid degradation of fibrin-based scaffolds?
Using inhibitors to prevent degradation
Why might a fibrin-based scaffold encounter problems with shrinkage during tissue engineering?
Excessive initial concentration of fibrinogen and calcium
Which strategy can help address the possibility of squishing during sheet formation when using a fibrin-based scaffold?
Utilizing methods to ensure proper entrapment
What changes can be made to a fibrin-based scaffold to enhance its mechanical stiffness?
Adjusting the initial concentration of fibrinogen and calcium
Learn about the relationship between gelatin and collagen in the context of natural biomaterials. Explore whether gelatin is considered a protein or just a polypeptide and its applications in tissue engineering.
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