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2. ENVIRONMENTAL ChEMISTRy & TEChNOLOGy 2.1. Lectures

2. ENVIRONMENTAL ChEMISTRy & TEChNOLOGy 2.1. Lectures

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Chem. Listy, 102, s265–s1311 (2008) Environmental Chemistry & Technology<br />

P88 SuRGICAL POLyESTER FAbRIC<br />

IMPREGNATED by CROSS-LINKED<br />

COLLAGEN<br />

PAVeL FILKA, LUCY VOJTOVá and JOSEF JAnČář<br />

Brno University of Technology, Faculty of Chemistry,<br />

Institute of Materials Chemistry, Purkyňova 464/118, 612 00<br />

Brno, Czech Republic,<br />

xcfilka@fch.vutbr.cz<br />

Introduction<br />

Collagen is a widely applicable protein in medical applications.<br />

The main advantage of this biomaterial is its ability<br />

to create fibers with a high strength and stability by using different<br />

cross-linking agents or physical methods. Collagen’s<br />

significant properties are biocompatibility and resorbability in<br />

organism, which might be particularly used at surface modification<br />

of surgical fabrics based on polyester silk (PES). The<br />

collagen modified PES nets used in surgery for longtime fixation<br />

or reinforcing different organs may accelerate healing<br />

injury as well as reduce inflammation of a tissue surrounding<br />

the implanted fabrics 1 .<br />

natural crosslinking gives collagen special properties,<br />

namely higher rigidity and endurance against proteolytical<br />

cleavage. However, during processing and utilization the<br />

collagen loses those particular properties. That is why the<br />

collagenous material is additionally cross-linked by chemical<br />

or physical methods in order to regenerate original net<br />

behaviours.<br />

Chemical methods employ bifunctional compounds<br />

(e.g. aldehydes, epoxides, isocyanides, carbodimides, acrylic<br />

acid etc.) which can react with amino groups of collagen<br />

in two different places resulting in generation of a new<br />

strengthing bond. Their main disadvantage is toxicity of<br />

used chemicals 2 . Instead of toxic aldehydes it might be used<br />

nontoxic 1-ethyl-3-(-dimethylaminopropyl) carbodiimide<br />

(EDC), which is soluble in water. For reaction acceleration<br />

the n-hydroxysuccinimide (nHS) as catalyst can be added to<br />

the system with EDC 3 .<br />

In this work cross-linking agents based on melaminformaldehyde<br />

resin (named as LYOFIX and MH – 83) as<br />

well as carbodiimide (system EDC/nHS) were used for<br />

crosss-linking collagen impregnated on the polyester surgical<br />

net CHS 100. Swelling behaviours in the water and degradation<br />

at 37 °C in physiological solution with the purpose of<br />

increasing biocompatibility of commercial surgical net were<br />

examined.<br />

Experimental<br />

Modified derivative of alkylmelamineformaldehyde in<br />

aqueous solution (LYOFIX, Ciba, Hungary), hexamethylolmelamineformaldehyde<br />

resin (MH-83, Draslovka a.s. Kolin,<br />

CZ), 1-ethyl-3-3-dimethylaminopropyl)-carbodiimide hydrochloride<br />

(EDC, Sigma-Aldrich s.r.o.), n- hydroxysukcinimide<br />

(nHS 98 %, Sigma-Aldrich s.r.o.), na 2 HPO 4 . 12H2 O<br />

(Lach-ner a.s. CZ), collagen type I (8 %, VUP a.s., Brno),<br />

net for surgical purposes (CHS 100 – knitwork made from<br />

s516<br />

polyester silk, VUP a.s., Brno), ultra - clean demineralize and<br />

deionize MILIQ water (prepared in arrangement of Millipore<br />

S.A. at FCH BUT, CZ).<br />

P r e p a r a t i o n o f a C o l l a g e n F i l m s<br />

Polyester fabric CHS 100 was cut into same size square<br />

pieces of about 1 cm 2 which were diped layed on the 5 ml<br />

of 1% collagen solution (prepared from 100% freeze – dried<br />

collagen) embedded with extra 5 ml of 1% collagen solution.<br />

This sample was air-dried for approximately 48 h to the constant<br />

weight.<br />

C r o s s - L i n k i n g<br />

Collagenous films were cross-linked by 2% solution<br />

of LYOFIX and Mn-83 resins for a period of 12 mins.<br />

Subsequently the samples were five times washed by the<br />

distilled water for 5 mins and dryied by air to the constant<br />

weight.<br />

Collagenous films were cross-linked by the ethanol solution<br />

containing 50 mmol dm –3 of EDC and 25 mmol dm –3 of<br />

nHS. After 4 h of cross-linking the samples were washed out<br />

for 2 h in 0.1M solution of na 2 HPO 4 . 12H2 O and finally four<br />

times for half an hour in the distilled water followed by airdrying<br />

to the constant weight.<br />

S w e l l i n g<br />

Swelling characteristics were evaluated to compare the<br />

cross-linking effectivity by each agent. Swelling proceeded<br />

for a period of 40 min to 1 h in MILIQ water at a laboratory<br />

temperature. Quantity of absorbed water was weighted in five<br />

minute intervals. Both water content (OV) and swelling ratio<br />

(SB) of each sample were calculated according to equation<br />

(1) and (2), where mc is weight of swollen sample in a given<br />

time and ms is weight of dry sample prior the swelling 4 .<br />

m<br />

OV [%] =<br />

c −ms<br />

⋅ 100<br />

(1)<br />

mc SB [–] = m c<br />

m s<br />

D e g r a d a t i o n<br />

Each sample was placed in the physiological solution<br />

with addition of sodium azide (0.1% naCl + 0.02% na 3 n)<br />

and placed into the incubator set to 37 °C to determine the<br />

hydrolytic degradation. Prepared samples were every day<br />

taken out from the incubator, dried by the filtration paper,<br />

consequently weighted and immediately placed back with<br />

fresh physiological solution. Degradation was expressed as<br />

percentual decrease of collagen weight in certain time having<br />

the zero point at the maximum of swelling according to equations<br />

(3) and additionaly (4)–(6).<br />

(2)

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