COLLAGEN

Structure, Important Properties, Important Derivatives and

Biomedical Applications

Guided By: Presented By:

Dr. Narayan Chandra Mishra Pawan Kumar Pandey
Associate professor PhD Scholar
Dept. of Polymer and Process Eng. Dept. of Polymer and Process Eng.
IIT Roorkee IIT Roorkee
 Contents

C 1.Introduction
O 2.Structure
L
3.Important Properties
L
4.Important Derivatives
A
5.Biomedical Applications
G
E 6.References

N
 Introduction

C
O
L
L
A
G
E
N
Superabundant fibrous protein that constitutes most of the extracellular matrix (ECM) in all animals.
 Introduction

C • Several types of collagen

O can be extracted from

mammalian tissues, fish,
alligators, and so forth.
L
• Native collagens are
L insoluble in organic
solvents due to their
A hydrophilicity with poor
mechanical strength.
G • Thus recombinant collagen

E are produced using

microbial systems to
improve mechanical
N strength.
 Introduction

C Intercellular
Cell

O Glue

L Cell

L
Cell
Cell

A Cell

G
Cell
E Cell

N The semantic origin of the term “collagen” is originated from the Greek term “Kolla,” which means
glue because collagen acts as an intercellular glue by inhibiting tissues from stretching or damaging.
 Introduction

C >30%
O Collagen

L Total
Protein
L <70%

A other
proteins

G
E
N Most abundant protein of human body. This biological polymer is the main component of
connective tissues, corresponding to more than 30 % by weight of the total proteins in the
animal body.
 Introduction

C
O
Overall,
L collagen
L guarante
A es tissues
G and
E organs'
N structura
l
 History

C
O
L
L
A
G
E
N Major milestone associated
with collagen in the
biomedical section.
 Collagen's sources

C
O
L
L
A
G
E
N
FIGURE-2: The sources of collagen
 Structural Hierarchy

C
O
L
L
A
G
E FIGURE 3: The hierarchical structure of
collagens (from amino acid sequence level

N
at nano-meter (nm) scale to collagen fibrils
and fibres with a micro-meter (µm) scale.
 Structural Organization
• Triple chain of Polyamide

C • ~1000 amino acid residues in each chain x 3 chains

• Every third residue is glycine
• Proline is also present to a much greater extent than in most other proteins
O • 4-Hydroxyproline is also present which is rarely found elsewhere

L The repeating tripeptide unit is Gly-X-Y, where X

may be any amino acid and Y is Proline or

L
Hydroxyproline. About 100 tropocollagen molecule stalked
Polymer of repeating tripeptide adopts a helical together to form a thin wire like structure
structure having 3 amino acids per turn. with a dimension of few µm x 100 nm

A
G Amino Acid Polyamide Triplex Helix Collagen Fibril Collagen Fibre

E
N
Collagen fibrils arrange together
Collagen 3 Polyamide chains join together by weak
in a wired manner to form a
= 35% Glycine + 11% interactions and form a tropocollagen
complete, fully functional
Alanine + 25% Proline/ molecule (unit of collagen), which has
collagen fibre having a
Hydroxyproline dimension of 300nm x 1.5 nm
dimension of few mm x 10 µm
 Structural Hierarchy
Primary Structure (Peptide

C
sequence)

O Secondary Structure (α-

helix)

L
L Tertiary Structure (3D-
arrangement of units)

A
G Quaternary Structure (Linking
of Sub-units)

E
N Collagen Fibre
 Structural Family of Collagen
Collagen Type Class Distribution Pathology

C I Fibrillar Dermis, bone, tendon, ligament Ehlers-Danlos Syndrome, osteoporosis

Osteoarthrosis, Chondrodysplasias

O
II Fibrillar Cartilage, vitreous

III Fibrillar Skin, blood, vessels, intestine Ehlers-Danlos syndrome, arterial Aneurysms

L IV Network Membranes Alport syndrome

L
V Fibrillar Bone, dermis, cornea, placenta Ehlers-Danlos, syndrome

VI Network Bone, cartilage, Cornea, dermis Bethelm, myopathy

A VII Anchoring, fibrils Dermis, bladder Epidermolysis Bullosa acquisita

VIII Network Fuchs endothelia, corneal dystrophy

G
Dermis, brain, Heart, kidney

fibril-associated collagen
IX with interrupted triple Cartilage, cornea, vitreous Osteoarthrosis, multiple epiphyseal Dysplasia

E X
helices

Network Cartilage Chondrodysplasia

N XV Multiplexing Capillaries, testis, kidney, heart —

fibril-associated collagen
XX with interrupted triple Cornea (chick) —
helices
 Collagen: Structural Derivatives

C COLLAGEN
DERIVATIVES
O
BASIS = DEGREES OF
L HYDROLYSIS

L UNDENATURED
COLLAGEN
GELATINE HYDROLYSATE
A COLLAGEN (UC)
(CH)

G NON-HYDROLYZED
PARTIALLY COMPLETELY
HYDROLYZED HYDROLYZED
E
MOLECULAR MOLECULAR
N MOLECULAR
WEIGHT = 300 kDa
WEIGHT OF 20- WEIGHT OF 2-
90 kDa 9 kDa
 Collagen: Functional Derivatives
1. Collagen is hydrophilic and possesses poor mechanical strength, demanding
C modification procedures to improve physicochemical and mechanical
properties for final applications, such as bone regeneration.
O
2. Collagen derivatives are most closely replicate the structural and better
L mechanical properties of native collagen. Collagen derivatives have non-toxicity
and minimal immunogenicity.
L
3. Additionally, collagen derivatives provides mechanical strength to the tissue
A and is a logical choice for a base scaffold support structure.

G 4. Collagen derivatives support cell adhesion and cell proliferation, making them
more attractive than some synthetic materials.
E
5. Common Collagen derivatives are fibers, gels, spheres, membranes, and
N sponges.
 Collagen: Biodegradation

C Highly Stable protein. (Lifetime about 6 months or higher)

O Collagen triple helix- resistant for proteases like pepsin, trypsin and chymotrypsin.

L Sensitive for various metalloproteinases

L
A
G
E
N
 Important Collagen Derivatives and their Biomedical Applications
Biomedical Applications
Biomedical Applications
C •
•
Drug delivery
Dialysis
• Cosmetic skin solutions
• Drug delivery

O
• Vitreous substitution
• Tissue regeneration Gel • Surgery
• Eye-shield (cornea) • Coats for prostheses
L • Skin adhesives
Biomedical Applications

L Membrane Sponge
• 3D cell culture
• Wound dressing

A Collagen
Derivatives
• Hemostatic agent
• Skin substitution

G
• Drug delivery
• Bone repair (rigid form)

E Biomedical Applications
• Microcarrier for cell Sphere
Hollow
fiber
Biomedical Applications
N
tubing
culture
• Cell culture
• Drug delivery
• Nerve regeneration
 Collagen Resources and Biomedical Application

C
O
L
L
A
G
E
N
 References

C 1. Rezvani Ghomi, E., Nourbakhsh, N., Akbari Kenari, M., Zare, M., & Ramakrishna, S.
(2021). Collagen‐based biomaterials for biomedical applications. Journal of Biomedical
Materials Research Part B: Applied Biomaterials, 109(12), 1986–1999.
O https://doi.org/10.1002/jbm.b.34881

L 2. Healy, K. E., Hutmacher, D. W., Grainger, D. W., Kirkpatrick, C. J., & Ducheyne, P. (2017).
Comprehensive Biomaterials II. Elsevier Gezondheidszorg.
L
A
G
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T H A N K
Y O U