Heparin intercalation into reconstituted collagen I fibrils: Impact on growth kinetics and morphology

Stamov, Dimitar R.; Grimmer, Milauscha; Salchert, Katrin; Pompe, Tilo; Werner, Carsten

doi:10.1016/j.biomaterials.2007.09.009

Cited by 69 publications

(83 citation statements)

References 80 publications

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“…Proline and hydroxyproline residues are abundant and account for approximately 22% of the amino acid residues [3,4] . The structure, assembly, and supramolecular aggregation of type Ⅰ collagen are the prototype from which our understanding of collagenous structure has developed, particularly fibrillar collagens [5] .Collagens have been used commercially as biomaterials in numerous medical applications involving hemostasis, wound repair and controlled release of drugs [6,7] . Tissue engineering has recently made great progress and an increasing number of researchers are using collagen as a scaffold for cell growth [1,[8][9][10] .…”

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confidence: 99%

Extraction and isolation of type I, III and V collagens and their SDS-PAGE analyses

Yuan

et al. 2011

Trans. Tianjin Univ.

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Abstract： Type Ⅰ, Ⅲ and Ⅴ collagens were extracted from bovine dermis and cornea by using pepsin treatment in acetic acid solution, followed by salt precipitation and dialysis, to purify and isolate each type of collagens. The preparation process was analyzed by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). A reducing agent, 2-mercaptoethanol, was used to remove disulfide bonds and analyze the structure of the bonds involved between α chains in some types of collagens. The use of delayed reducing methods resulted in the difference between α1(Ⅲ) and α1(Ⅰ) chains in a mixture containing type Ⅰ and Ⅲ collagens. The structure of disulfide bonds among α chains exists potentially in type Ⅴ collagen prepared from the pepsin-treatment extraction at 4 ℃, which differs from type Ⅲ collagen in relation to the locations of disulfide bonds. Compared with pepsin-treated collagen at 4 ℃, the relative molecular weights of α1(Ⅴ) and α2(Ⅴ) chains treated at room temperature decrease by 4.6% and 6.0%, respectively. It is concluded that type Ⅰ, Ⅲ and Ⅴ collagens can be prepared from bovine dermis and cornea by the use of pepsin treatment, salt precipitation and dialysis. The interchain disulfide bonds lie potentially near the edges of termini of type Ⅴ collagen molecules in extracellular matrix, and a small number of interchain crosslinks exist in type Ⅴ collagen.Collagen is a main constituent protein of extracellular matrix (ECM), and it exists widely in dense connective tissue. Studies on the changes in the mechanical and structural properties of collagen, relating to its preparation, will not only help improve the use of collagen in the biomedical field, but also improve our understanding of the biological characteristics of ECM [1,2] . At least 27 types of collagen molecules, which are encoded by different genes, have been discovered (designated from Ⅰ to ⅩⅩⅦ). The primary cha-racteristic structure of polypeptides adopting collagenous triple-helical structures consists largely of the repeated sequence Gly-X-Y, where Gly represents glycine and X or Y is any other amino acid residue. Proline and hydroxyproline residues are abundant and account for approximately 22% of the amino acid residues [3,4] . The structure, assembly, and supramolecular aggregation of type Ⅰ collagen are the prototype from which our understanding of collagenous structure has developed, particularly fibrillar collagens [5] .Collagens have been used commercially as biomaterials in numerous medical applications involving hemostasis, wound repair and controlled release of drugs [6,7] . Tissue engineering has recently made great progress and an increasing number of researchers are using collagen as a scaffold for cell growth [1,[8][9][10] . This relates to the preparation, structure and properties of collagens, specifically the structural modifications for a desired characteristic.Type Ⅰ, Ⅲand Ⅴ collagens used in this paper are fibrillar collagens, which are characterized by an uninterrupted helical domain of approximately 300 nm in ...

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confidence: 99%

Extraction and isolation of type I, III and V collagens and their SDS-PAGE analyses

Yuan

et al. 2011

Trans. Tianjin Univ.

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“…The heparin is known to intercalate with the collagen due to its very strong electronegativity. [16] The mixing of the two solutions results in formation of intercalation, but would gradually be separated from each other. Then, the collagen would starts to fibrillize by the existence of inorganic salts, resulting in the increase in the opacity.…”

Section: Resultsmentioning

confidence: 99%

Preparation Fibrillized Collagen‐Glycosaminoglycan Complex Matrix Using Fibrillogenesis

Nam

Kimura

Kishida

2015

Macromolecular Symposia

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Summary: In order to replicate the function of the native dermis, we prepared fibrillized collagen-GAGs complex matrix possessing the similar structure as native dermis structure using collagen re-arrangement phenomenon in the physiological conditions. For GAGs, hyaluronic acid, chondroitin-6-sulfate, and heparin were used. In the process of preparing a collagen-GAGs complex matrix, the fibrillization of the collagen was observed when hyaluronic acid and chondroitin-6-sulfate were mixed together with collagen in the physiological conditions. However, no fibrillization was observed when collagen was mixed with heparin to prepare a collagen-heparin complex matrix. The swelling ratio and the mechanical strength had changed by the fibrillization, where low water absorption and brittleness was shown for collagenheparin complex matrix which is not fibrillized. This study shows that hyaluronic acid and chondroitin-6-sulfate contributes to the fibrillization of the collagen while the heparin forms intercalation with collagen molecules preventing fibrillogenesis.

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“…Hyaluronic acid (Davidenko et al, 2010) Matrix, membrane, hydrogel, fibers Silk fibroin (Zhou et al, 2010) Membrane, fibers, matrix, microtubes Chondroitin-6-suphate (Stadlinger et al, 2008) Tube, matrix Elastin Tube, film, fibers, matrix Alginate (Sang et al, 2011) Spongious, filler for bone, Chitosan (Sionkowska et al, 2004) Matrix, membrane, tubular graft, nanofibers, hydrogel, Heparin (Stamov et al, 2008) Matrix Collagensynthetic polymer Poly-L-lactide (PLLA) (Chen et al, 2006) Coating for composite Poly-lactic-co-glycolic-acid (PLGA) (Wen et al, 2007) Fibers, matrix, coated tube ε-caprolactone (Schnell et al, 2007) Nanofibers Poly(ethylene-glycol) (PEG) Films, fibers…”

Section: Type Of Composite Type Of Component From Composite Compositementioning

confidence: 99%

Collagen-Based Drug Delivery Systems for Tissue Engineering

Albu¹,

Titorencu²,

Ghica³

2011

Biomaterials Applications for Nanomedicine

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Heparin intercalation into reconstituted collagen I fibrils: Impact on growth kinetics and morphology

Cited by 69 publications

References 80 publications

Extraction and isolation of type I, III and V collagens and their SDS-PAGE analyses

Extraction and isolation of type I, III and V collagens and their SDS-PAGE analyses

Preparation Fibrillized Collagen‐Glycosaminoglycan Complex Matrix Using Fibrillogenesis

Collagen-Based Drug Delivery Systems for Tissue Engineering

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