1/10/2011

Higher expectations of quality of life
Rising standards of living 
TTL 746 Changing attitude

2004: number of people aged over 60 amounts to 
p p
40% of the entire population.
Medical Textiles 2009:  66.57 years 

Textile products that have been engineered to

meet specific needs of suitable medical &
surgical applications, related to hygiene &
healthcare

Minor 1

Overview‐ Classification of Med Textile field Course structure

Polymers & fibres 
Design criteria  &  fabrication methods
Non‐implantable materials:  Wound dressing, Bandages, Gauges
Implantable biomedical devices: Hernia mesh, Vascular grafts, Sutures, Heart valves Minor 1:     25%
Minor 2
Scaffolds for Tissue Engineering : Minor 2:     25%     (Open book)
Cartilage (nonwoven, 3D weaving) ,   Skin (nonwoven, weaving)  , Liver
(rapid prototyping) Kidney Urinary bladder (nonwoven 3D weaving)
(rapid prototyping) ,   Kidney, Urinary bladder    (nonwoven, 3D weaving) , 
Tendons, Ligaments    (Silk filaments, braiding),    Cornea 
Major:
Major:         35‐
35 40%
Major Quiz, Term report:   10‐15%
Healthcare & hygiene products: Surgical Gown, mask, wipes, Antibacterial
Textile, Super absorbent polymer, Dialysis, adhesive, anti‐adhesive patches for Term Paper  :    students should identify existing specific 
Surgical application, Hollow fibre bioreactors, Coating & finishing technologies
clinical problems of any Medical Textile product, & propose 
Characterizing tests, Evaluation of commercial Med Textiles products,  novel solutions using ‘smart’ Medical Textiles.
Standards….. Legal & ethical issues
(3 students per group)

• Papers to be distributed in class Hottest future professions of the twenty‐first century

Time Magazine online, 
• Medical Textiles, by Subhash Anand,Woodhead Publishing Ltd http://www.time.com/time/magazine/article/0,9171,997028,00.html
• Medical Textiles and Biomaterials for Healthcare, Ed
by S.C. Anand, M Miraftab, JF Kennedy, Woodhead Publishing Ltd,
2005

• Medical Textile monthly newsletters, Technical Textiles Net

Publications

• Medical Textiles 2007: Proceedings of 4th Int conf on healthcare and

medical textiles,
By JF Kennedy, SC Anand, M Miraftab, S Rajendran, CRC Press

• Principles of Tissue Engineering, by Lanza, Langer, Vacanti

• Tissue Engineering Journal, Mary Ann Liebert Inc. Publications

May, 2000

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Tata Economic Consultancy Services road map for Indian Technical Textile sector
Market size of Technical textiles in India 
Market Size & Potential Market Size & Potential
(Rs. Crore) (Rs. Crore)
1.  TISSUE  ENGINEERS S.
Technical
Textile Sector Assumed
2003-04 2007-08 2005-06 growth rate 2014-15
2.  GENE  PROGRAMMERS  No (Actual) per (Predicted)
annum (%)
3.  Genetic Eng FARMERS   1 Clothtech 6833 8415 7583 15 26677
2 Packtech 4602 7359 5152 12 14288
3 Indutech 2212 2993 1148 12 3182
4 Sporttech 1534 2049 1773 15 6238
5  Meditech  1525  2339  1152  20 %  5945 
6 Mobiltech 1323 2046 1532 10 3613
7 Hometech 1029 1897 1398 15 4918
8 Agrotech 303 464 376 20 1938
...and which jobs will disappear? 9 Protech 284 638 819 10 1931
10 Buildtech 281 478 1333 20 6877
11 Oekotech 200 6732 42 10 98
Teachers 12 Geotextiles - 6591 999 10 2357
TOTAL 20128 42006 23307 14.37 78060

‘Technical Textiles and Industrial Nonwovens: World Market Forecast to 2010’ published by 
David Rigby Associates
Current Indian scenario
Sanitary napkins, baby & adult diapers : 35%
Surgical wound dressing :  30%
Sutures : 20%
Medical devices & other healthcare textiles: 15%
(angioplasty, bypass surgery, 
stent, compression garments, masks) 

• Consumption is increasing rapidly

• Private Hospitals, Health centres are rapidly growing
•Doctors/patients’ awareness for hygiene is increasing
• Medical tourism

Why Textiles should be used for Medical purpose?

Use of Textile‐based constructs for Med Textile & 
Tissue eng

1. Combinations of variety of designs – Fibre, yarns, polymers Safe but cheaper solutions

Greater freedom to optimize design and performance

Major challenges ahead:
2 Easy handling,
2. handling manipulation by surgeon
1. Innovative designing
3. Flexibility, supplenss, mechanical strength similar to soft
2. Better understanding of structure‐function relationship
tissues
3. Multidisciplinary approach of problem solving
4. Fatigue resistance to survive dynamic motions inside body
4. GMP for Biological testing – in vitro, in vivo studies
5. Porous structures of fabric will allow tissue in growth
5. Ethical regulations & Funding

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What Constitutes Medical Textiles ? Medical Textiles

Polymers (& Liq crystals, hydrogels)– Biocompatible
Non‐ Implantable Implantable Healthcare
Chemicals – Medical Products materials materials products

Fibres & Yarns ‐ Normal, Functional
Fabrics – Woven, Non‐woven, Knitted, Braided Suture Scaffolds for 
Tissue
F b i ti
Fabrication  Techniques
T h i – Molding, Casting
M ldi C ti engineering

Products and Technologies

Chemistry,  Fibre Technol,  Textile Engineering,  
Mechanical Eng,          Computer Sci, 
Product development,        Biology,    Biotechnology, 
Instrumentation & Biomed Eng

Non‐implantable materials Implantable materials

Examples of some exciting Medical Textiles

Cornea
Cornea(Knitting, Electrospinning,
Hydrogel composite)
Sewing ring fabric
Blood vessels(Electrospinning,
vessels
Knitting, Braiding)
Muscle
(Electrospinning, Knitting, Cardiac tissue(knitting)
tissue
Fibrous composite)
Liver(Rapid prototyping)
Liver

Nerve
Kid
Kidney, U
Urinary
i bl
bladder
dd
(Electrospinning,
(Nonwoven, 3D weaving)
Rapid prototyping)

Tendons, Ligaments
(Mono/multi-filaments, Braiding)
(Nonwoven, Weaving)Skin
Skin

Cartilage(Nonwoven, 3D
Cartilage
weaving)
Commercially available 
Knitted heart valve
valve
developed at IITD

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Cardiac Constraint sock for congestive heart failure

Acorn cardiovascular Inc

Polypropylene or polyester mesh used

for hernioplasty and pelvic floor surgery

Biocompatible Polymers
Ease of processing ‐ versatility of options
Improve strength ‐ orientation, fibre‐hydrogel composites, crosslinks

Bio‐inert Å……….Æ degradable

FDA Approved synthetic biodegradable polymers ( “ for  specific  
applications” )

PLA, PGA,  PLGA,        Poly(caprolactone),    Polydioxanone 

Biodegradable polymers derived from natural sources 
modified polysaccharides (cellulose, chitin, dextran, alginate) 
Silk, 
modified proteins (fibrin, casein)

Fibres are present even within a cell !! Collagens & Elastins: the proteins of 

connective tissues.     
tendons and ligaments.

Keratins: proteins that are major 
components of skin, hair, feathers and 
horn.

Fibrin: a protein formed when blood 
clots.

De Humnai Corporis Fabrica Libri
Collagen fibre Andreas Vesalius (1514–1564) 

Globular Proteins Fibrous Proteins Nerve fibres

1543 Basel
Elastinfibres Switzerland
Fibrous proteins are insoluble in water, due to a high percentage of hydrophobic amino
Muscle fibres
acids in their primary structures.

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Courtesy: Prof M Spector, MIT
The major ECM molecules present in tissues

1. Collagen fibres.

2 Elastinfibres
2.  Elastinfibres.

3. Proteoglycans and glycosaminoglycans (GAGs).

4. Cell‐adhesion molecules (fibronectin, laminin, etc).

5.  Water (about 65%). 
Collagen fibres in Extra cellular matrix of cartilage

Protein fibres are polymers of amino acids 30% of the human proteins consist of collagen

Two amino acids can be covalently joined by a amide linkage (Peptide Bond) Collagen is the basic building material of fibrous connective tissue of living organisms.

Orientation of collagen fibres determines the 
mechanical behavior of the tissue.
Uniaxialorientation in tendon, 
ligament
Random orientation in skin

wavyy fiber morphology

p gy g
gives extensibility
y

Parallelyoriented collagen fibres Randomly oriented collagen fibres on skin 

Bone is a composite-
hydroxyapatite reinforced by collagen
fibers.
Large blood vessels are interpenetrating
networks of elastin fibers and collagen
fibers.

Orientation of collagen fibres in Cornea govern transparency Collagen molecules produced by the cells self‐assemble into fibres.

These fibres provide functional integrity of tissues.

Cells in our body produce small collagen fibres

Characteristics of collagen fibres: 
digitation on surface

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Collagen fibresare fibrous proteins with a unique amino acid

composition rich in glycine, proline, and hydroxyproline

20 different amino acids…… 6 types of collagen fibres. 

Collagen I : striated fibres…….. Blood vessel wall, tendons, ligaments, 
bone
80‐160 nm in dia
high tensile str  ( Young’ s mod 1 X 109 Pa )
Collagen II :< 80 nm dia…… cartilage, intervertebral disc
Collagen IV  : abundant in Basement membrane
Collagen VI : joins cells with surrounding matrix Gopalasamudram Narayana Iyer Ramachandran (1922-2001)
Ramachandran plot is a way to visualize dihedral angles phi against psi of amino
residues in protein structures. it shows the possible conformation of of phi and psi
angles for a polypeptide.

Primary structure:  complete sequence of amino acids in the 
polypeptide chain. Scale: 1 nm.
Secondary structure: single peptide stands that are fold to recurring
structural patterns.…..Alpha‐helix, beta‐sheet, beta‐turn    Scale: 10 nm

Tertiary structure:   Three helical polypeptide units twist to form a 
triple‐helical collagen molecule: 
a molecular “rope”   which has some bending stiffness and does not 
undergo rotation.
Quaternary structure: Several collagen molecules pack side‐by‐side 
in a highly specific register to give a crystalline fiber with a 64 to 67‐
nm periodicity (collagen banding pattern)….. H-bonding, salt
bridges, disulfide bonds
Differences in protein function result from differences in amino acid composition
and sequence.
Metalloprotein enzyme Collagenase degrades collagen fibers. collagen fibrils: 10-300 nm

Melting of collagen to gelatin (loss of tertiary structure) spontaneously follows such  Collagen fibres: few μm

degradation.

Mechanism of collagen fibril assembly Elastin   fibres

Intracellular : mRNA - Endoplasmic Reticulum- protein synthesis-
3 proto-alpha- chains form soluble procollagen
fibrous protein acts to impart elasticity and resilience to
tissue
Extracellular
C- terminal propeptides Present in walls of large arteries, lungs, skin
N-terminal
by pro-peptidase enzyme It is more compliant than collagen
Young’s mod 3 X 109 Pa

A network of randomly coiled macromolecules

( glycine, proline, but no hydroxylysine ) .

Highly extensible chains: alternating stretchy hydrophobic segments of beta-

structure & rigid hydophilic segments of alpha-helix structure

Stretching of elastin fibers leads to large entropy loss due to reduction

in chain configurations & increased “ordering” of water molecules
against nonpolar amino acids. Spontaneous retraction

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Silk primary sequences and secondary structures

alanine,
glycine-alanine,
glycine-alanine-serine

Pupa

Sericin
(protein) Fibroin
(protein)

crystalline β-sheets: contribute to the high tensile strength of

silk fibers
β-turn, helical structures: provide elasticity
20~30 μm

Silk Courtsey: Prof D Kaplan, Tufts Why Silk is suitable for Medical applications ?

DIAMETER     <100  (i) Biocompatibility: Silk sutures (FDA approved),         biocompatible, 

MORPHOLOGY – surface area μm Æ microns  less immunogenic and inflammatory than collagens or polyesters such as PLGA  
PEO
(ii)  Stability &Mechanical Properties: remarkable strength & toughness, compressive 
strength and modulus…… which exceed other commonly used degradable 
polymeric biomaterials. 
CRYSTALLINITY 
Processing Options 
Processing Options
for Protein  thermal stability ‐ can be autoclaved without loss of mechanical integrity 
Protein‐Based 
Biomaterials CHEMICAL DECORATION ‐ cell 
Biomaterials – silk functions ‐
stabilized by   beta sheet secondary structures which are physical crosslinks formed via 
hydrogen bonding and 
β‐sheets
hydrophobic interactions via inter‐ and intra‐chain interactions.
MINERALIZATION –
composites ‐
(iii) Modifiable: chemical decoration with RGD peptide, BMP2 and other cell    
modulating factors  using facile carbodiimide coupling 

attachment of antimicrobial peptides.
Silica RGD BMP2
hydroxyapatite (iv) Slow Degradability: fast (weeks) to very slow (years) 

Seaweed – brown algae
Alginate Azotobactervinelandii, Pseudomonas

Egg box model

Ca2+ Ca2+ Ca2+ Ca2+

Ca2+
Ca2+
Ca2+

Fibrepropertiesdepend on ratio of G and M  Ca2+
High G contentgivesmorebrittlegels, not good forfibreproduction.
High M contentgivesmoreelasticgels.

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Method of isolation
Cospinning of Alginate with other polysaccharides (such as 
Seaweed + 0.1‐ 0.2 N mineral acid  chondroitin sulphate, dermatan sulphate, heparan sulphate or 
heparin) 
Neutralization with NaOH
(Qin Y, Gilding DK, Advanced Medical Solutions Limited (GB) , Fibres 
of cospun alginates, 
Precipitation in CaCl2
Parameters:   United States Patent 6,080,420 , June 27, 2000 )
NaCl/CaCl2 ratio, 
Exposure time,
Concentration & mol weight of modifiers
Degradation
Preparation of Alginate fibre for wound care
Lyases (bacteria, fungi) specifically 
Wet spinning of alginate fibres containing 25% w/w branan ferulate 1% w/v  depolymerise alginate
concentration of calcium chloride.

( Miraftab M, Qiao Q, Kennedy JF, Groocock MR, Anand SC, Advanced wound 
care materials: developing an alginate fibre containing branan ferulate. J 
Wound Care. 2002;11(9):353‐6 )

Method of isolation
Chitosan Dil NaOH Dil acid
Waste crab shell Deproteinization Demineralization

Chitosan Chitin Decoloration

crustacean, insects, fungi, yeasts
Method of Chitosan fibre preparation
chitosan dissolved in aq. 1‐2% (v/v) acetic acid by stirring at room temp 
Chitin, 
overnight.
poly[ β(1→4)‐2‐acetoamido‐2‐deoxy‐ D‐glucopyranose]

non‐toxic, non‐allergenic, anti‐microbial, and biodegradable  Plasticizer (e.g., PEG, Glycerol) at 1‐2% (w/w) concentration added (optional) 

filtered and injected into a coagulation bath at 40oC containing a mixture of 30% 0.5 
Deacetylation of chitin by alkali  M Na2SO4, 10% 1M NaOH and 60% distilled water.
generates chitosan

Fibers kept in this coagulation medium for 1 day & washed with distilled water. 
poly[ β(1→4)‐2‐amino‐2‐deoxy‐D‐glucopyranose]
Fibres are suspended in aq. 30% methanol for 4–5 hr & in 50% methanol overnight.
Extent of deacetylation governed by alkali conc and time of reaction. Hudson SM, Review of Chitin and Chitosan as fibre and film formers, J 
Degree of deacetylation & MW influence characteristics of chitosan Mater Sci, Mater Med, C34(3) 375‐437, 1994

‘‘Intelligent’’ or ‘‘smart’’ materials
Smart Hydrogels are water‐swollen polymeric networks containing 
chemical or physical crosslinks, which can undergo volume 
Chitin and chitosan can be degraded by Lysozyme, Papain 
transitions in response to minute changes in environmental 
stimuli such as pH , ionic strength , temperature or electric fields  which acts slowly to depolymerise the polysaccharide. 
etc.
Chitosan is known to degrade in human serum in vitro.
pH sensitive‐ness of Chitosan 
Insoluble Soluble
Alginate Ca2+,     <pH 2  EDTA, > pH 2
The biodegradation rate of the polymer is determined by 
Chitosan > pH 6.5 < pH 6.5 the amount of residual acetyl content. 

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Hyaluronic acid Degradation 

Hyaluronidase

Hyaff‐11 :     degradation time of around 40 days

Alternating   β‐1,4    and    β‐1,3 glycosidic bonds
During in vivo degradation Hyaff‐11 fibres 
Hyaff‐11: an esterified form of hyaluronan. become  more and more hydrophilic, 
forming a gel similar to native hyaluronan found 
The esterification process results in a highly  in the extracellular matrix. 
hydrophobic polymer that can be spun, or woven.
Fidia Advanced Biopolymers, Italy