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Ghosh and Yi
Table 2. (Continued).
Biomaterials Derived from Compositions Advantages Disadvantages Reference
mechanical iii. The fact that
disruption. decellularization
causes
non-reversible
secondary structural
changes in collagen
is commonly
overlooked by
researchers.
Silk There are many The fibroin chain is i. Mechanism of i. As the amino [92]
different forms made up of amino- (N-) biomineralization acid sequences of
of silk fibroin (130 amino acids) and ii. Structural fibroins are diverse
in nature, yet carboxyl- (C-) (100 amino modification is among different
those generated acids) peptide domains; simple. species, either due
from silkworm whereas the C-terminus iii. under control to environmental
and spider silk is conserved in both envionment impacts or
are the most silkworms and spiders, the iv. Possibility of evolution,
studied. Due to N-terminus is conserved introducing batch-to-batch
its widespread only in spiders, and the physical variance exists.
availability, sequence in silkworms crosslinks ii. For optimal
silkworm silk varies greatly. (-sheets) to printability, it must
Bombyx mori is cause sol-to-gel be mixed with
unquestionably transitions without another polymer.
the better known using solvents, iii. The rheology of
of the two major heat, or UV light. the bioink must be
sources. v. High cellular optimized.
viability for at
least 1 month
vi. Adaptable
structural
modification
Gelatin Gelatin Gelatin is composed of 18 i. Phase transition i. Mechanically weak [92,104]
is mainly different types of complex behavior in a at physiological
derived from amino acids, the most thermo responsive temperatures
mammalian important of which are system ii. Stability of printed
cells. The glycine, hydroxyproline, ii. Encourages constructions
primary sources proline and with the cellular necessitates the
of gelatin are remainder consist of other proliferation and incorporation of
collagens from well-known amino acid the production of polymeric dopants
pigs, cows, families such as glutamic ECM. or crosslinking.
Sometimes, acid, alanine, arginine, and iii. Low
gelatine can also aspartic acid. immunogenicity.
be extracted Gelatin’s chemical structure
from the skin also includes α-chains (one
and bones of polymer/single chain),
various kinds of β-chains (two covalently
fish. crosslinked α-chains), and
γ-chains (three covalently
crosslinked α-chains)
with molar masses of
approximately 90×10 ,
3
180×10 , and 300×10 g/mol,
3
3
respectively.
International Journal of Bioprinting (2022)–Volume 8, Issue 4 185