Abstract:Biomaterial science has made enormous progress in the last few decades. Nonetheless, innovative biomaterials are still urgently needed to provide in vitro cell-culture models that more closely resemble three-dimensional (3-D) cell interactions and cyto-architectures in bodies and tissues. In this review, the recent advances toward this goal through molecular engineering of various designer self-assembling peptide scaffolds are discussed. These peptide scaffolds can be commercially and custom-tailor synthesized… Show more
“…For example, a peptide hydrogel functionalized with bone marrow homing peptide in addition to RADA16 not only enhanced cell attachment but also promoted neural stem cell differentiation without the addition of soluble growth factors. 17 These experiments demonstrate the applicability of attaching a functional peptide motif to RADA16. In these experiments, however, the functionalized self-assembling peptides were chemically synthesized, presenting a limitation for functional motifs that can fuse to RADA16.…”
Section: Introductionmentioning
confidence: 74%
“…RADA16 spontaneously assembles in the presence of monovalent salt or under physiological conditions as a result of both the ionic side chain interactions and the conventional b-sheet propensity of the backbone, ultimately forming a macroscopic hydrogel known to facilitate cell culture. 14,[16][17][18] Cell attachment and neurite outgrowth were enhanced when neural cells were cultured on this hydrogel. Moreover, cells may be embedded in RADA16 peptide hydrogels, providing a 3-D environment for the cells to grow.…”
Peptides were genetically produced that were composed of two or three repeats of the self-assembling peptide RADA16 (RADARADARADARADA), and referred to as RADA16 Â 2 and RADA16 Â 3, respectively. These peptides were expressed as fusion proteins that retained the activity of the fusion partner protein. The expressed peptides exhibited both fibril formation and the ability to support cell adhesive activity. Moreover, hydrogels formed by the peptides via the addition of a medium provided a three-dimensional environment for cell proliferation. Polymer Journal (2013) 45, 504-508; doi:10.1038/pj.2012.216; published online 12 December 2012Keywords: 3-D cell culture; genetically synthesis; hydrogel; self-assembling peptide
INTRODUCTIONThe development of biomaterials that support cellular functions, such as cell adhesion, growth and differentiation, is important for tissue engineering. 1 In an effort to create such novel biomaterials, artificial extracellular matrices (ECMs) have been developed by various groups. [2][3][4][5] Artificial ECM proteins have been designed and genetically synthesized in our laboratory. 6-10 Our strategy for the design of artificial ECM proteins relies on the combination of structural peptides and active functional peptides that control cellular functions. One of the ECM proteins previously constructed in our lab, named ERE, is composed of 12 repeats of the elastin-derived APGVGV peptide motif as the stable structural peptide, with the cell adhesive RGD peptide motif as the active functional peptide. 6,7 ERE can be immobilized on a hydrophobic surface via the hydrophobic APGVGV peptide motif and exhibits cell adhesive activities as a result of the RGD peptide. Multi-functional ECM proteins have also been constructed based on the ERE protein. EREI, which consists of ERE fused with the IKVAV peptide, not only exhibits cell adhesive activity but also promotes angiogenesis and neural differentiation as a result of the combination of IKVAV and RGD. [8][9][10][11][12] In our genetic engineering-based designs, multi-functional ECMs composed not only of peptide motifs but also of growth factors were constructed. Epidermal growth factor fused to the ERE protein was found to exhibit cell growth activity via the epidermal growth factor moiety. 7 Our genetically designed ECM proteins based on ERE demonstrated applicability as biomaterials. 6-10 However, covalent cross-linking is required to form a hydrogel structure in order to
“…For example, a peptide hydrogel functionalized with bone marrow homing peptide in addition to RADA16 not only enhanced cell attachment but also promoted neural stem cell differentiation without the addition of soluble growth factors. 17 These experiments demonstrate the applicability of attaching a functional peptide motif to RADA16. In these experiments, however, the functionalized self-assembling peptides were chemically synthesized, presenting a limitation for functional motifs that can fuse to RADA16.…”
Section: Introductionmentioning
confidence: 74%
“…RADA16 spontaneously assembles in the presence of monovalent salt or under physiological conditions as a result of both the ionic side chain interactions and the conventional b-sheet propensity of the backbone, ultimately forming a macroscopic hydrogel known to facilitate cell culture. 14,[16][17][18] Cell attachment and neurite outgrowth were enhanced when neural cells were cultured on this hydrogel. Moreover, cells may be embedded in RADA16 peptide hydrogels, providing a 3-D environment for the cells to grow.…”
Peptides were genetically produced that were composed of two or three repeats of the self-assembling peptide RADA16 (RADARADARADARADA), and referred to as RADA16 Â 2 and RADA16 Â 3, respectively. These peptides were expressed as fusion proteins that retained the activity of the fusion partner protein. The expressed peptides exhibited both fibril formation and the ability to support cell adhesive activity. Moreover, hydrogels formed by the peptides via the addition of a medium provided a three-dimensional environment for cell proliferation. Polymer Journal (2013) 45, 504-508; doi:10.1038/pj.2012.216; published online 12 December 2012Keywords: 3-D cell culture; genetically synthesis; hydrogel; self-assembling peptide
INTRODUCTIONThe development of biomaterials that support cellular functions, such as cell adhesion, growth and differentiation, is important for tissue engineering. 1 In an effort to create such novel biomaterials, artificial extracellular matrices (ECMs) have been developed by various groups. [2][3][4][5] Artificial ECM proteins have been designed and genetically synthesized in our laboratory. 6-10 Our strategy for the design of artificial ECM proteins relies on the combination of structural peptides and active functional peptides that control cellular functions. One of the ECM proteins previously constructed in our lab, named ERE, is composed of 12 repeats of the elastin-derived APGVGV peptide motif as the stable structural peptide, with the cell adhesive RGD peptide motif as the active functional peptide. 6,7 ERE can be immobilized on a hydrophobic surface via the hydrophobic APGVGV peptide motif and exhibits cell adhesive activities as a result of the RGD peptide. Multi-functional ECM proteins have also been constructed based on the ERE protein. EREI, which consists of ERE fused with the IKVAV peptide, not only exhibits cell adhesive activity but also promotes angiogenesis and neural differentiation as a result of the combination of IKVAV and RGD. [8][9][10][11][12] In our genetic engineering-based designs, multi-functional ECMs composed not only of peptide motifs but also of growth factors were constructed. Epidermal growth factor fused to the ERE protein was found to exhibit cell growth activity via the epidermal growth factor moiety. 7 Our genetically designed ECM proteins based on ERE demonstrated applicability as biomaterials. 6-10 However, covalent cross-linking is required to form a hydrogel structure in order to
“…4, 23, 24, 25, 26, 27, 28, 29
β ‐sheet peptides are of particular interest as they allow the fabrication of very stable hydrogels with properties that can be tailored through peptide design, media properties and processing. We have recently investigated the self‐assembly and gelation properties of a family of β ‐sheet peptides 30, 31, 32, 33, 34 based on the design developed by Zhang and co‐workers.…”
“…Since then, the rapid development of this type of self-assembling peptide has fostered numerous applications, including three-dimensional (3D) cell culture, tissue engineering, regenerative medicine, and sensory devices. [25][26][27] This peptide has one side group with charged side chains and another side group with hydrophobic chains. In water, the charged side is exposed on the outside and the hydrophobic side forms a double sheet inside the nanofiber.…”
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.