Journal of Archives in Military Medicine Journal of Archives in Military Medicine J Arch Mil Med http://www.jammonline.com 2345-5071 2345-5063 10.5812/jamm en jalali 2017 6 23 gregorian 2017 6 23 4 4
en 10.5812/jamm.42367 The Effect of Cross-Linking Agents and Collagen Concentrations on Properties of Collagen Scaffolds The Effect of Cross-Linking Agents and Collagen Concentrations on Properties of Collagen Scaffolds research-article research-article Results

The results confirmed that the extracted collagen is pure and free of any non-collagen protein contamination. Furthermore, the results showed that average pore size of the scaffolds from EDC/NHS cross-linker with molar ratio of 1:1 (I) was less than the scaffolds that were made using EDC/NHS cross-linker with molar ratio of 2:1 (II). Moreover, collagen samples that were cross-linked using 1:1 EDC/NHS molar ratios showed increased mechanical strength comparing to 2:1 EDC/NHS molar ratio.

Background

Collagen-based scaffolds are appealing products for various applications in pharmaceutics and tissue engineering and military applications like wound healing.

Objectives

This study was conducted to extract acid soluble collagen protein from calf skin tissue and cross-linked it using cross-linking agents. The collagen scaffolds with different 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) / N-hydroxysuccinimide (NHS) molar ratios as cross-linking agents were investigated.

Methods

The type I extracted collagen was used as a raw material for making collagen based scaffolds. Different EDC/NHS molar ratios as cross-linking agents were used. Matrix morphology and mechanical strength of the scaffolds were determined to evaluate the physicochemical properties of the collagen matrices with different cross-linker molar ratios. Furthermore collagen and cross-linked collagen were characterized using standard methods like SDS- page, FT-IR and SEM analysis.

Conclusions

The applied protocol is a convenient method for extraction of collagen and obtaining pure calf skin collage type I. Furthermore the best molar ratio of EDC/NHS cross-linking agents to cross-link collagen is 1:1 for obtaining stronger collagen structure.

Results

The results confirmed that the extracted collagen is pure and free of any non-collagen protein contamination. Furthermore, the results showed that average pore size of the scaffolds from EDC/NHS cross-linker with molar ratio of 1:1 (I) was less than the scaffolds that were made using EDC/NHS cross-linker with molar ratio of 2:1 (II). Moreover, collagen samples that were cross-linked using 1:1 EDC/NHS molar ratios showed increased mechanical strength comparing to 2:1 EDC/NHS molar ratio.

Background

Collagen-based scaffolds are appealing products for various applications in pharmaceutics and tissue engineering and military applications like wound healing.

Objectives

This study was conducted to extract acid soluble collagen protein from calf skin tissue and cross-linked it using cross-linking agents. The collagen scaffolds with different 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) / N-hydroxysuccinimide (NHS) molar ratios as cross-linking agents were investigated.

Methods

The type I extracted collagen was used as a raw material for making collagen based scaffolds. Different EDC/NHS molar ratios as cross-linking agents were used. Matrix morphology and mechanical strength of the scaffolds were determined to evaluate the physicochemical properties of the collagen matrices with different cross-linker molar ratios. Furthermore collagen and cross-linked collagen were characterized using standard methods like SDS- page, FT-IR and SEM analysis.

Conclusions

The applied protocol is a convenient method for extraction of collagen and obtaining pure calf skin collage type I. Furthermore the best molar ratio of EDC/NHS cross-linking agents to cross-link collagen is 1:1 for obtaining stronger collagen structure.

Collagen;Scaffold;Cross-link Collagen;Scaffold;Cross-link http://www.jammonline.com/index.php?page=article&article_id=42367 Majid Jafari-Sabet Majid Jafari-Sabet Department of Pharmacology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran; AJA University of Medical Sciences, Tehran, Iran; Pharm D, PhD, Department of Pharmacology, School of Medicine, Iran University of Medical Sciences (Iums), Tehran, Iran. Tel: +98-2186703120 Department of Pharmacology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran; AJA University of Medical Sciences, Tehran, Iran; Pharm D, PhD, Department of Pharmacology, School of Medicine, Iran University of Medical Sciences (Iums), Tehran, Iran. Tel: +98-2186703120 Habib Nasiri Habib Nasiri AJA University of Medical Sciences, Tehran, Iran; Department of Medical Genetics, Nika Center for Health Promotion and Preventive Medicine, Tehran, Iran AJA University of Medical Sciences, Tehran, Iran; Department of Medical Genetics, Nika Center for Health Promotion and Preventive Medicine, Tehran, Iran Ramin Ataee Ramin Ataee Pharmaceutical Sciences Research Center, Mazandaran University of Medical Sciences, Sari, Iran Pharmaceutical Sciences Research Center, Mazandaran University of Medical Sciences, Sari, Iran