SKIN STRUCTURE AND ITS

COMPONENTS
Md. Saidur Rahman Shakil
Lecturer
ILET, DU
Summary of Collagen Triple Helix
• Collagen is composed of three chains, wound together in a tight triple helix. A repeated
sequence of three amino acids forms this sturdy structure. Every third amino acid is glycine, a
small amino acid that fits perfectly inside the helix. Many of the remaining positions in the chain
are filled by two unexpected amino acids: proline and a modified version of proline,
hydroxyproline.
• At least twenty nine types of collagen (designated) are found in vertebrates.
• • The best-known types (I, II, and III) each consist of 3 polypeptides, called α chains. Each chain
has the general structure (Gly-X-Y)330, with the 3 chains wrapped around each other in a
ropelike triple helix.

• • Type I collagen consists of 2 identical α chains (α1), and a slightly different chain, called (α2).
•
Hierarchy of collagen structure
The structure of all skins used in leather manufacture consists of basically a number
of collagen fibrils that group together in a rope to form fibers and fiber bundles. The
fiber bundles weave in amongst each other 3D to form a very strong yet highly
flexible structure.
Collagen fibril: The smallest unit of collagen structure fibrils are too small to be
resolved by light microscopy, electron microscopy is required. The triple helices are
bound together in bundles called fibrils.
Fibril bundle: Fibrils are grouped together to create fibril bundles.
Fiber: A grouping together of fibril bundles.
Fiber bundle: Fibers come together to create fiber bundles.
Collagen
Protein molecules consist of hundreds or thousands of amino acids joined together by the
polypeptide linkages. These polypeptide chains may be folded in a variety of different
ways and each protein molecules give individual proteins their characteristic properties.
One such distinguished protein is collagen. Collagen is the major fibrous element of hides
and skins, in fact, it is the most abundant protein in the animal kingdom, making up from
25% to 35% of the whole-body protein content. . Due to its physicochemical properties,
collagen is responsible for the integrity, strength and elasticity of tissues.
Importance of collagen in the leather industry:
Collagen actually forms the main part of the skins and hides that are treated in the tanning
process and its structure is part of the reason behind leather’s unique properties. During
the beam house phase, all the fats, oils, and hair in the skin are removed, leaving the
collagen framework behind as the basis for leather. During the tanning process, the
collagen is cross-linked and that is where a hide turns into stable leather that retains
flexibility and resistant properties.
Properties of collagen
There are more than 28 types of collagen identified. Collagen types I, II, III are the most abundant. However,
over 90% of the collagen found in the body, hides, and skins is type I. The variations are due to the
differences in the assembly of basic polypeptide chains, different lengths of the helix.
What is type Collagen type I:
It is a protein found in skin, tendon, organs, and bone tissues. Collagen types I is the principal connective
tissue proteins of the dermal tissues and are abundant in tendon, bone, and blood vessels.
The collagen molecules (tropocollagen) are about 280 nm long, about 1.5 nm in diameter,
o It has a molecular weight of about 300000.
o They are composed of three polypeptide chains which are twisted together in form of a helix (triple helix)
and which consist of amino acids that are linked together by peptide bonds.
Chemically, collagen has an unusual amino acid composition and the sequence of the constituent amino
acids. Some of the common chemical properties of collagen are given below:
1. The number of glycine residues amounts to 1/3 of all amino acid residues. Its content of glycine
proline, hydroxyproline is characteristic in many ways.
2. Collagen will not break down in water solution, but it may be dissolved in a strong acid solution. It is
also be dissolved by strong alkali.
• Fibre bundles composed of fibres (20 – 200 μm in diameter) which in turn consist of elementary
fibres (about 5 μm in diameter), and these of fibrils (10 – 100 nm in diameter), and these of
microfibrils (about 5 nm in diameter), and these of macromolecules.
 Physical and physiochemical properties of Collagen:
– Whitish, hard, and brittle in the dry state.
– Insoluble in cold water and organic solvents.
– Water absorption up to 70% of its original weight;
– Water vapor absorption up to 50% on the collagen weight. Decisive advantages over synthetic
replacement materials.
– Preservation by dehydration is possible.
– With continuous heating in the presence of water, the fibers shrink to one-third of their original length
and begin to cement together irreversibly. The Specific temperature at which collagen start to shrink is
called Ts temperature.
▪ It has unique properties: it remains soft and flexible under low stress and stiffens when stress is
increased.
– Collagen shows minimum swelling at the isoelectric point.
– Dilute acids and alkalis cause swelling due to the charge, i. e. volume and weight increase owing to
higher water uptake (reversible, almost no change in the structure of collagen). An increase in
temperature and concentration and extension of time results in swelling due to hydrolysis.
• Fibrous structure of skin (collagen)

• The fundamental basic unit is called as tropocollagen.

o The tensile strength of collagen is remarkable: a fiber 1 mm in diameter can hold a load of 10 to 40 kg without breaking.
o Collagen is physiologically stable. Disruption of fibrils only begins at temperatures above 50 C. Onset of the transition
occurs at (58 +/-10) C and the main transition occurs at (65 +/- 10) C.
o The main transition corresponds to the process of gelatinization of collagen in a hydrated environment and is caused by the
breaking of internal cross-links

• 1 kg raw skin has a reactive inner fibre surface area of 1000 – 2500 meter square.
• Another unusual feature of collagen is the presence of a branched chain.
• Anisotropic nature of skin/hide:
• The skin/hide matrix is composed of a three dimensional (3D) weave of collagen fibre bundles.
The collagenmolecules have a triple helical structure with 3 × 10−5 cm length and 15 × 10−8 cm
diameter, which are basic building blocks in the formation of skin/hide . Hierarchical organization
of collagen in skin .
• Collagen fibre bundles present in the corium minor are more compactly woven and smaller in
diameter than those present in corium major.
• There are variations in compaction of weave, angle of weave; pore properties with respect to area
of skin/leather.
• In addition to this, there are variations across the cross-section for a given area.
• Therefore, skin/leather is generally ‘anisotropic’ in nature. Due to the different levels of
organisation of collagen in skin different pore dimensions are existing.
Keratin
Another important type of protein present in raw hides and skins is keratin, which composes the skins’ outer
layer. Thus hairs, nails, hooves, feathers, etc are all composed of keratin. The amount of keratin. The amount of
keratins in skins varies with species and also with age.

Properties of keratin:
1. Keratin is very stable to hot water and mild chemical attacks. The stability of keratin is due to the presence of
cystine. Cystine is an amino acid containing sulfur. This sulfur forms a stable sulfur-sulfur linkage between
protein hairs.
2. keratins have a characteristic sulfur content of 3 – 5% (disulfide bridge of cystine).

3. Hydrolytically splittable by reduction and oxidation.