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Collagen Tissue Engineering: Development of Novel Biomaterials and Applications

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Collagen Tissue Engineering: Development of Novel Biomaterials and Applications 0031-3998/08/6305-0492 Vol. 63, No. 5, 2008 PEDIATRIC RESEARCH Printed in U.S.A. Copyright © 2008 International Pediatric Research Foundation, Inc. Collagen Tissue Engineering: Development of Novel Biomaterials and Applications LIAN CEN, WEI LIU, LEI CUI, WENJIE ZHANG, AND YILIN CAO Department of Plastic and Reconstructive Surgery [W.L., L.C., W.Z., Y.C.], Shanghai 9th People’s Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China; National Tissue Engineering Center of China [L.C., W.L., L.C., W.Z., Y.C.], Shanghai 200235, China ABSTRACT: Scientific investigations involving collagen have in- regeneration is to restore both the structural integrity and the spired tissue engineering and design of biomaterials since collagen vivid remodeling process of native ECM, especially restoring the fibrils and their networks primarily regulate and define most tissues. delicate collagen networks under which normal physiologic re- The collagen networks form a highly organized, three-dimensional generation occurs. architecture to entrap other ingredients. Biomaterials are expected to Collagen molecules have a triple-helical structure and the function as cell scaffolds to replace native collagen-based extracel- lular matrix. The composition and properties of biomaterials used as presence of 4-hydroxyproline resulting from a posttransla- scaffold for tissue engineering significantly affect the regeneration of tional modification of peptide-bound prolyl residues provides neo-tissues and influence the conditions of collagen engineering. The a distinctive marker of these molecules (2). To date, 28 complex scenario of collagen characteristics, types, fibril arrange- collagen types have been identified; I, II, III, and V are the ment, and collagen structure-related functions (in a variety of con- main types that make up the essential part of collagen in bone, nective tissues including bone, cartilage, tendon, skin and cornea) are cartilage, tendon, skin, and muscle. They also exist in fibrillar addressed in this review. Discussion will focus on nanofibrillar forms with elaborate 3D arrays in ECM (3–5). assemblies and artificial synthetic peptides that mimic either the Bone tissues are mainly constructed from type I with a fibrillar structure or the elemental components of type I collagen as small quantity of type V collagen forming a framework that illustrated by their preliminary applications in tissue engineering. anchors nanosized hydroxyapatite (HA) crystals. Both organic Conventional biomaterials used as scaffolds in engineering collagen- containing tissues are also discussed. The design of novel biomate- and mineral phases compose a closely interwoven and highly rials and application of conventional biomaterials will facilitate complex but ordered composite which is further organized development of additional novel tissue engineering bioproducts by into layers, or lamellae, that are a few microns thick. The refining the currently available techniques. The field of tissue engi- lamellae are arranged into higher order structures. The organic neering will ultimately be advanced by increasing control of collagen in framework is mainly constructed by type I collagen fibrils in native tissue and by continual manipulation of biomaterials. (Pediatr elaborate 3D arrays as concentric weaves (4), and the anchored Res 63: 492–496, 2008) bone crystals are 50 nm long, 28 nm wide, and 2 nm thick (6). Bioengineered bone was formed by collagen synthesis, GENERAL DESCRIPTION ON COLLAGEN IN fibril formation, assembling and crosslinking with mineraliza- CONNECTIVE TISSUES tion by Ca-P crystals to form a continuous network and further remodeling. Collagen fibers, while providing the framework The extracellular matrix (ECM), provides physical support to for HA deposits, are the principal source of tensile strength of tissues by occupying the intercellular space, acting not only as bone tissues. The mechanical properties of bone can be ad- benign native scaffolding for arranging cells within connective justed by varying fibril orientation which may result from the tissues, but also as a dynamic, mobile, and flexible substance degree of collagen crosslinking and the mineral-organic com- defining cellular behaviors and tissue function (1). For most posite remodeling process (7,8). soft and hard connective tissues (bone, cartilage, tendon, cornea, There are three main types of cartilage: hyaline articular blood vessels, and skin) collagen fibrils and their networks cartilage, fibrocartilage, and elastic cartilage. This review will function as ECM, the highly organized, three-dimensional (3D) only discuss hyaline articular cartilage which is found on the architecture surrounding various cells. Collagen plays a dominant surface of long bones in articulating joints and is extremely role in maintaining the biologic and structural integrity of ECM important in the lubrication and load distribution in the joint. and is highly dynamic, undergoing constant remodeling for Usually, articular cartilage is subdivided into three zones: proper physiologic functions (1). Hence, the ideal goal of tissue superficial, middle, and deep zones (9). Type II collagen is the chief component in articular carti- Received October 31, 2007; accepted January 4, 2008. lage and is approximately 60% of the dry weight of the tissue. Correspondence: Yilin Cao, M.D., Ph.D., Department of Plastic and Reconstructive Surgery, Shanghai 9th People’s Hospital, Shanghai Jiao Tong University School of Medicine, 639 Zhi Zao Ju Road, Shanghai, 200011, P. R. China; e-mail: [email protected] Abbreviations: DBM, demineralized bone matrix; ECM, extracellular ma- This study is financially supported by National “973 ” (2005CB522700), and Shanghai Pu Jiang Foundation of Shanghai Science and Technology Development Committee trix; GAG, glycosaminoglycans; HA, hydroxyapatite; PA, peptide-amphi- (07pj14110, to L.C.). phile; PGA, polyglycolide 492 SCAFFOLDS FOR COLLAGEN TISSUE ENGINEERING 493 According to the work by Muir et al., small fibers with a strength to the stroma. The 3D architecture of the thin collagen diameter of less than 10 nm are distributed in all of its three fibrils may contribute to cornea transparency (21). zones (10). There are also large fibers of approximately 34 nm The complex structure of fibrillar type I collagen presents in diameter, oriented parallel to the surface in the superficial different morphologies in different tissues performing different zone; fibers of 70–100 nm mostly arranged randomly in the functions. When associated with HA crystals in bone, it middle zone; fibers of ϳ140 nm organized radially in the deep provides rigid and shock-resistant tissues with high Young zone. Trace amounts of types I, VI, IX, X, and XI collagens modulus. It can behave like an elastomer with low rigidity and can also be detected (11). high deformation to rupture in tendon. In cornea, it shows Collagen fibers, together with 10% glycosaminoglycans optical properties such as transparency. Capturing the intrinsic (GAGs), contribute to the viscoelasticity and compressive building blocks and more complex, higher order supramolecu- function of articular cartilage, although the three zones differ lar structures of collagen has been the current focus of the in their viscoelastic and compressive properties. Assuming biomaterial society. that different aligning patterns and distribution of collagen fibers account for this difference, cartilage engineering relies DEVELOPMENT OF NOVEL BIOMATERIALS on successful engineering of collagen frameworks in different zones for further deposition of other proteins, especially pro- In view of the variety of roles played by collagen in teoglycans or GAGs. different tissues, research has focused on developing novel Tendon consists of type I fibrillar collagen along with trace biomaterials to mimic the intricate fibrillar architecture which quantities of types II, III, IV, V, and VI and is 60–85% would be able to function as cell scaffolding replacing native collagen by dry weight. Tendon transmits the force of mus- collagen-based ECM. cular contraction to bone (9,12) and most tendon types expe- One promising candidate is peptide-amphiphile (PA) nano- rience tension, such as Achilles or patellar tendon, although a fibers which are produced by molecular self-assembly as few types also experience a certain degree of compression, developed by Stupp and coworkers (22,23). The self- such as the supraspinatus tendon (13). Collagen fibrils in assembling unit is a PA, a hydrophilic 11-residue peptide with tendon vary in diameter from 30 nm to 300 nm, depending on an N-terminal alkyl tail of 16 carbon atoms. PAs are synthe- the stage of development (14). Usually a nonuniform or sized by standard solid phase chemistry that ends with the bimodal distribution of fibril diameters can be observed, alkylation of the NH2 terminus of the peptide and they further which allows for tight lateral packing (15). These fibrils are self-associate to form cylindrical micelles or nanofibers be- generally oriented longitudinally to support the great tensile cause of the amphiphile’s overall conical shape. The alkyl tails stress exerted on the tissue although some may be transversely are packed in the centers of the fibers, while the peptide arranged (9,16). Collagen fibrils are essential in tendon for segments are exposed to the aqueous environment so the maintaining mechanical properties and for transmitting force chemistry of the peptide region is repetitively displayed on during movements (5). their surface. The
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