Guide to collagen characterization for biomaterial studies

被引:122
作者
Abraham, Leah C. [1 ,2 ,3 ]
Zuena, Erin [1 ,2 ,3 ]
Perez-Ramirez, Bernardo [4 ]
Kaplan, David L. [1 ,2 ,3 ]
机构
[1] Tufts Univ, Dept Chem, Medford, MA 02155 USA
[2] Tufts Univ, Dept Biol Engn, Medford, MA 02155 USA
[3] Tufts Univ, Dept Biomed Engn, Bioengn & Biotechnol Ctr, Medford, MA 02155 USA
[4] Genzyme Corp, BioFormulat Dev, Framingham, MA 01701 USA
关键词
collagen; characterization; denatured; structure; biomaterials;
D O I
10.1002/jbm.b.31078
中图分类号
R318 [生物医学工程];
学科分类号
0831 [生物医学工程];
摘要
The structure and remodeling of collagen in vivo is critical to the pathology and healing of many human diseases, as well as to normal tissue development and regeneration. In addition, collagen matrices in the form of fibers, coatings, and films are used extensively in biomaterial and biomedical applications. The specific properties of these matrices, both in terms of physical and chemical characteristics, have a direct impact on cellular adhesion, spreading, and proliferation rates, and ultimately on the rate and extent of new extracellular matrix formation in vitro or in vivo. In recent studies, it has also been shown that collagen matrix structure has a major impact on cell and tissue outcomes related to cellular aging and differentiation potential. Collagen structure is complex because of both diversity of source materials, chemistry, and structural hierarchy. With such significant impact of collagen features on biological outcomes, it becomes essential to consider an appropriate set of analytical tools, or guide, so that collagens attained from commercial vendors are characterized in a comparative manner as an integral part of studies focused on biological parameters. The analysis should include as a starting point: (a) structural detail-mainly focused on molecular mass, purity, helical content, and bulk thermal properties, (b) chemical features-mainly focused on surface elemental analysis and hydrophobicity, and (c) morphological features at different length scales. The application of these analytical techniques to the characterization of collagen biomaterial matrices is critical in order to appropriately correlate biological responses from different studies with experimental outcomes in vitro or in vivo. As a case study, the analytical tools employed for collagen biomaterial studies are reviewed in the context of collagen remodeling by fibroblasts. The goal is to highlight the necessity of understanding collagen biophysical and chemical features as a prerequisite to (a) studies with cells and tissue formation, and (b) suggest modes to establish comparative outcomes for studies conducted in different laboratories. (C) 2008 Wiley Periodicals, Inc.
引用
收藏
页码:264 / 285
页数:22
相关论文
共 136 条
[1]
Impact of collagen structure on matrix trafficking by human fibroblasts [J].
Abraham, LC ;
Vorrasi, J ;
Kaplan, DL .
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, 2004, 70A (01) :39-48
[2]
Phagocytosis and remodeling of collagen matrices [J].
Abraham, Leah C. ;
Dice, J. Fred ;
Lee, Kyongbum ;
Kaplan, David L. .
EXPERIMENTAL CELL RESEARCH, 2007, 313 (05) :1045-1055
[3]
Extracellular matrix remodeling - Methods to quantify cell-matrix interactions [J].
Abraham, Leah C. ;
Dice, J. Fred ;
Finn, Patrick F. ;
Mesires, Nicholas T. ;
Lee, Kyongbum ;
Kaplan, David L. .
BIOMATERIALS, 2007, 28 (02) :151-161
[4]
Alberts B., 2002, Molecular Biology of The Cell, V4th
[5]
Altankov G, 1996, J BIOMED MATER RES, V30, P385, DOI 10.1002/(SICI)1097-4636(199603)30:3<385::AID-JBM13>3.0.CO
[6]
2-J
[7]
Engineering of osteochondral tissue with bone marrow mesenchymal progenitor: Cells in a derivatized hyaluronan-gelatin composite sponge [J].
Angele, P ;
Kujat, R ;
Nerlich, M ;
Yoo, J ;
Goldberg, V ;
Johnstone, B .
TISSUE ENGINEERING, 1999, 5 (06) :545-553
[8]
Awad HA, 2000, J BIOMED MATER RES, V51, P233, DOI 10.1002/(SICI)1097-4636(200008)51:2<233::AID-JBM12>3.0.CO
[9]
2-B
[10]
Enhanced triple helix stability of collagen peptides with 4R-aminoprolyl (Amp) residues:: Relative roles of electrostatic and hydrogen bonding effects [J].
Babu, IR ;
Ganesh, KN .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (09) :2079-2080