Collagen is the main structural component of extracellular matrix (ECM) in many biological tissues. On the basis of its peculiar physico-chemical properties it is considered the highest module protein in connective tissue. Reconstituted collagen fibers have been obtained from single molecule collagen suspensions telopeptides-free following three different routes: either by changing the pH solution or by electrochemically assisted deposition or by electrospinning methods. For all the applications, type I collagen was extracted from horse Achilles tendon using the standardized manufacting method of OPOCRIN SpA and made clear of glycosaminoglycan fraction. The first route is based on the collagen auto-assembling properties using a sol/gel type reaction to yield collagen fibrils, identified by SDS-PAGE analysis, which organize in network through freeze-drying. The second route leads to electrochemically-assisted deposition of collagen fibrils on Ti plates by an electrolytic process: to purely helical collagen molecules suspended in 0.9 wt% NaCl water solution a constant current for different periods of time is apllied at room temperature.
Biomimetic reconstituted collagen fibers from molecular suspensions
FOLTRAN, ISMAELA;FORESTI, ELISABETTA;MANARA, SILVIA;ROVERI, NORBERTO;SABATINO, PIERA;TOSI, GIOVANNA
2007
Abstract
Collagen is the main structural component of extracellular matrix (ECM) in many biological tissues. On the basis of its peculiar physico-chemical properties it is considered the highest module protein in connective tissue. Reconstituted collagen fibers have been obtained from single molecule collagen suspensions telopeptides-free following three different routes: either by changing the pH solution or by electrochemically assisted deposition or by electrospinning methods. For all the applications, type I collagen was extracted from horse Achilles tendon using the standardized manufacting method of OPOCRIN SpA and made clear of glycosaminoglycan fraction. The first route is based on the collagen auto-assembling properties using a sol/gel type reaction to yield collagen fibrils, identified by SDS-PAGE analysis, which organize in network through freeze-drying. The second route leads to electrochemically-assisted deposition of collagen fibrils on Ti plates by an electrolytic process: to purely helical collagen molecules suspended in 0.9 wt% NaCl water solution a constant current for different periods of time is apllied at room temperature.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
