title: Biomimetic soluble collagen purified from bones.
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.
authors: Department of Mechanical and Aerospace Engineering, Politecnico di Torino, Turin, Italy.
authors: Ana Marina
authors: AM
authors: Ferreira
authors: Piergiorgio
authors: P
authors: Gentile
authors: Susanna
authors: S
authors: Sartori
authors: Cristina
authors: C
authors: Pagliano
authors: Chiara
authors: C
authors: Cabrele
authors: Valeria
authors: V
authors: Chiono
authors: Gianluca
authors: G
authors: Ciardelli
mesh_terms: D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry / Q000302:isolation & purification; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism*; D001842:Bone and Bones / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D024042:Collagen Type I / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D004492:Edetic Acid / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005269:Femur / Q000737:chemistry; D010434:Pepsin A / Q000737:chemistry; D011817:Rabbits; D012867:Skin / Q000737:chemistry; D013057:Spectrum Analysis; D013816:Thermodynamics; D013977:Tibia / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D024042:Collagen Type I; D004492:Edetic Acid; D010434:Pepsin A