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Biomimetic soluble collagen purified from bones

Lookup NU author(s): Dr Ana Ferreira-Duarte, Dr Piergiorgio Gentile

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Abstract

Type I collagen has been extensively exploited as a biomaterial for biomedical applications and drug delivery; however, small molecular alterations occurring during the isolation procedure and its interaction with residual bone extracellular matrix molecules or proteins might affect the overall material biocompatibility and performance. The aim of the current work is to study the potential alterations in collagen properties and organization associated with the absence of proteoglycans, which mimic pathological conditions associated with age-related diseases. A new approach for evaluating the effect of proteoglycans on the properties of isolated type I collagen from the bone matrix is described. Additional treatment with guanidine hydrochloride was introduced to remove residual proteoglycans from the collagen matrix. The properties of the isolated collagen with/without guanidine hydrochloride treatment were investigated and compared with a commercial rabbit collagen as control. We demonstrate that the absence of proteoglycans in the isolated type I collagen affects its thermal properties, the extraction into its native structure, and its ability to hydrate and self-assemble into fibers. The fine control and tuning of all these features, linked to the absence of non-collagenous proteins as proteoglycans, offer the possibility of designing new strategies and biomaterials with advanced biomimetic properties aimed at regenerating bone tissue in the case of fragility and/or defects


Publication metadata

Author(s): Ferreira AM, Gentile P, Sartori S, Pagliano C, Cabrele C, Chiono V, Ciardelli G

Publication type: Article

Publication status: Published

Journal: Biotechnology Journal

Year: 2012

Volume: 7

Issue: 11

Pages: 1386-1394

Print publication date: 01/11/2012

Online publication date: 15/08/2012

Acceptance date: 23/07/2012

Publisher: Wiley-Blackwell Publishing Ltd.

URL: http://dx.doi.org/10.1002/biot.201200184

DOI: 10.1002/biot.201200184


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