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. 2019 Jan 28;303(3):408–426. doi: 10.1002/ar.24067

Table 1.

An overview of “Biomaterials” section, natural polymers.

Natural* , ** Pro Contra
(Glyco)proteins Fibrin

‐ Injectable

‐ Suitable for bioprinting

‐ High elasticity

‐ High stability

‐ Cell adhesive sequence***

Mechanically weak
Silk fibroin

‐ Outlasts structural integrity of Fibrin and collagen

‐ Controllable mechanical properties

‐ Suitable for bioprinting, mixture with gelatin

‐ Stiffness comparable to brain tissue

Adhesive properties have to be added
Fibronectin

‐ Cell adhesion properties ***

‐ Ability to sequester nutrients and growth factors

‐ Produced by patients own cells

‐ Used as a coating of synthetic polymers

Laminin

‐ Injectable

‐ No need for gelation initiator

‐ Cell adhesive sequence both RGD and IKVAV***

Collagen

‐ Injectable

‐ Cell adhesive sequence***

‐ Successful in microfluidic systems

Harmful cell encapsulation conditions
Matrigel™

‐ Injectable

‐ Approved commercial product

‐ Several ECM proteins and growth factors present

‐ cell adhesion properties

Harmful cell encapsulation conditions
Polysaccharides Hyaluronic acid

‐ Adds compression strength, lubrication, and hydration to ECM

‐ injectable

‐ Control of permeability by methacrylation

‐ Stiffness comparable to brain tissue

‐ Stimulates angiogenesis

No cell adhesion motifs
Alginate

‐ Injectable

‐ Suitable for bioprinting

‐ No cell adhesion motifs

‐ Variable 3D structure

‐ Nonphysiological conditions during gelation

Chitosan

‐ Antimicrobial anti‐inflammatory

‐ Physiological cell encapsulation conditions when modified

‐ No cell adhesion motifs

‐ Poor solubility

Background information is indicated by symbols.

*

In almost all natural polymers there is a potential risk of pathogen transmission, because most of them are derived from animal sources.

**

Most natural polymers are subject to batch‐to‐batch variation, inhomogeneity and they are easily degraded in a physiological environment.

***

RGD adhesive motif may not always be exposed for integrin binding, this depends on the protein conformation (Bellis, 2011).