Self-assemble peptide biomaterials and their biomedical applications
TL;DR: This review outlines designs of self-assembly peptide (β-sheet, α-helix, collagen-like peptides, elastin-like polypeptides, and peptide amphiphiles) with potential additional functionalities and their biomedical applications in bioprinting, tissue engineering, and drug delivery.
About: This article is published in Bioactive Materials.The article was published on 2019-02-13 and is currently open access. It has received 155 citations till now. The article focuses on the topics: Self-healing hydrogels.
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TL;DR: This review outlines recent progress in several bioprinting technologies used to engineer scaffolds with requisite mechanical, structural, and biological complexity and examines the process parameters affecting biop printing and bioink-biomaterials and concludes with the future perspective of biopprinting technology.
562 citations
TL;DR: In this paper, the authors discuss various methods that have been used to achieve gel-to-gel transitions by modifying a pre-formed gel material through external perturbation, and describe methods that allow time-dependent autonomous switching of gels into different networks enabling synthesis of next generation functional materials.
Abstract: Supramolecular gels are formed by the self-assembly of small molecules under the influence of various non-covalent interactions. As the interactions are individually weak and reversible, it is possible to perturb the gels easily, which in turn enables fine tuning of their properties. Synthetic supramolecular gels are kinetically trapped and usually do not show time variable changes in material properties after formation. However, such materials potentially become switchable when exposed to external stimuli like temperature, pH, light, enzyme, redox, and chemical analytes resulting in reconfiguration of gel matrix into a different type of network. Such transformations allow gel-to-gel transitions while the changes in the molecular aggregation result in alteration of physical and chemical properties of the gel with time. Here, we discuss various methods that have been used to achieve gel-to-gel transitions by modifying a pre-formed gel material through external perturbation. We also describe methods that allow time-dependent autonomous switching of gels into different networks enabling synthesis of next generation functional materials. Dynamic modification of gels allows construction of an array of supramolecular gels with various properties from a single material which eventually extend the limit of applications of the gels. In some cases, gel-to-gel transitions lead to materials that cannot be accessed directly. Finally, we point out the necessity and possibility of further exploration of the field.
131 citations
TL;DR: This review aims to summarize the recent advances in PLL-based nanomaterials in these biomedical fields over the last decade by describing the synthesis of PLL and its derivatives and the main text of their recent biomedical applications and translational studies.
84 citations
TL;DR: The advanced strategies for enhanced long-term lumen patency of vascular grafts are summarized in this review, which requires recruitment of endothelia progenitor cells (EPCs), migration, adhesion, proliferation and activation of EPCs and ECs,Anti-thrombogenesis, anti-IH, and immunomodulation are discussed.
82 citations
Cites background from "Self-assemble peptide biomaterials ..."
...1794 components are arranged into hierarchical organized structures spontaneously supported by non-covalent interactions [68]....
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TL;DR: This review covers the important aspects of peptide hydrogels as 3D scaffolds, including mechanical properties, biodegradability and bioactivity, and the current approaches in creating matrices with optimized features.
70 citations
References
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TL;DR: Two complementary strategies can be used in the fabrication of molecular biomaterials as discussed by the authors : chemical complementarity and structural compatibility, both of which confer the weak and noncovalent interactions that bind building blocks together during self-assembly.
Abstract: Two complementary strategies can be used in the fabrication of molecular biomaterials. In the 'top-down' approach, biomaterials are generated by stripping down a complex entity into its component parts (for example, paring a virus particle down to its capsid to form a viral cage). This contrasts with the 'bottom-up' approach, in which materials are assembled molecule by molecule (and in some cases even atom by atom) to produce novel supramolecular architectures. The latter approach is likely to become an integral part of nanomaterials manufacture and requires a deep understanding of individual molecular building blocks and their structures, assembly properties and dynamic behaviors. Two key elements in molecular fabrication are chemical complementarity and structural compatibility, both of which confer the weak and noncovalent interactions that bind building blocks together during self-assembly. Using natural processes as a guide, substantial advances have been achieved at the interface of nanomaterials and biology, including the fabrication of nanofiber materials for three-dimensional cell culture and tissue engineering, the assembly of peptide or protein nanotubes and helical ribbons, the creation of living microlenses, the synthesis of metal nanowires on DNA templates, the fabrication of peptide, protein and lipid scaffolds, the assembly of electronic materials by bacterial phage selection, and the use of radiofrequency to regulate molecular behaviors.
3,125 citations
Additional excerpts
...“- + - + - + -+” is modulus I; “–++–++” is modulus II; “—+++” is modulus III; and “——++++” is modulus IV [9]....
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TL;DR: The artificial nanofiber scaffold induced very rapid differentiation of cells into neurons, while discouraging the development of astrocytes, linked to the amplification of bioactive epitope presentation to cells by the nanofibers.
Abstract: Neural progenitor cells were encapsulated in vitro within a three-dimensional network of nanofibers formed by self-assembly of peptide amphiphile molecules. The self-assembly is triggered by mixing cell suspensions in media with dilute aqueous solutions of the molecules, and cells survive the growth of the nanofibers around them. These nanofibers were designed to present to cells the neurite-promoting laminin epitope IKVAV at nearly van der Waals density. Relative to laminin or soluble peptide, the artificial nanofiber scaffold induced very rapid differentiation of cells into neurons, while discouraging the development of astrocytes. This rapid selective differentiation is linked to the amplification of bioactive epitope presentation to cells by the nanofibers.
2,081 citations
"Self-assemble peptide biomaterials ..." refers background in this paper
...Promotion of nerve regeneration with elongated axonal and attenuated astrogliosis as well as reduced glia scarring were obtained [73,74]....
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TL;DR: Preliminary evidence from invertebrates is included which suggests that the principles for bipolar fibril assembly were established at least 500 million years ago, and how mature fibrils are assembled from early fibrILS is reviewed.
Abstract: Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained. How the fibrils are formed from their monomeric precursors is the primary concern of this review. Collagen fibril formation is basically a self-assembly process (i.e. one which is to a large extent determined by the intrinsic properties of the collagen molecules themselves) but it is also sensitive to cell-mediated regulation, particularly in young or healing tissues. Recent attention has been focused on "early fibrils' or "fibril segments' of approximately 10 microns in length which appear to be intermediates in the formation of mature fibrils that can grow to be hundreds of micrometers in length. Data from several laboratories indicate that these early fibrils can be unipolar (with all molecules pointing in the same direction) or bipolar (in which the orientation of collagen molecules reverses at a single location along the fibril). The occurrence of such early fibrils has major implications for tissue morphogenesis and repair. In this article we review the current understanding of the origin of unipolar and bipolar fibrils, and how mature fibrils are assembled from early fibrils. We include preliminary evidence from invertebrates which suggests that the principles for bipolar fibril assembly were established at least 500 million years ago.
1,438 citations
TL;DR: The strategies for using molecular self‐assembly as a toolbox to produce peptide amphiphile nanostructures and materials are highlighted and efforts to translate this technology into applications as therapeutics are reviewed.
Abstract: Peptide amphiphiles are a class of molecules that combine the structural features of amphiphilic surfactants with the functions of bioactive peptides and are known to assemble into a variety of nanostructures. A specific type of peptide amphiphiles are known to self-assemble into one-dimensional nanostructures under physiological conditions, predominantly nanofibers with a cylindrical geometry. The resultant nanostructures could be highly bioactive and are of great interest in many biomedical applications, including tissue engineering, regenerative medicine, and drug delivery. In this context, we highlight our strategies for using molecular self-assembly as a toolbox to produce peptide amphiphile nanostructures and materials and efforts to translate this technology into applications as therapeutics. We also review our recent progress in using these materials for treating spinal cord injury, inducing angiogenesis, and for hard tissue regeneration and replacement.
1,300 citations
"Self-assemble peptide biomaterials ..." refers background in this paper
...control the nanostructure assembling into cylindrical or fibril geometries instead of micelles [57,58]....
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TL;DR: This work has shown that a 16-residue peptide has a characteristic beta-sheet circular dichroism spectrum in water and spontaneously assembles to form a macroscopic membrane, which may be a model for studying the insoluble peptides found in certain neurological disorders.
Abstract: A 16-residue peptide [(Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)2] has a characteristic beta-sheet circular dichroism spectrum in water. Upon the addition of salt, the peptide spontaneously assembles to form a macroscopic membrane. The membrane does not dissolve in heat or in acidic or alkaline solutions, nor does it dissolve upon addition of guanidine hydrochloride, SDS/urea, or a variety of proteolytic enzymes. Scanning EM reveals a network of interwoven filaments approximately 10-20 nm in diameter. An important component of the stability is probably due to formation of complementary ionic bonds between glutamic and lysine side chains. This phenomenon may be a model for studying the insoluble peptides found in certain neurological disorders. It may also have implications for biomaterials and origin-of-life research.
1,221 citations
Additional excerpts
...Inspired by the self-assembling peptide amino acid sequence (Ac(AEAEAKAK)2-CONH2) found in the yeast protein zuotin [8], numerous designs of peptides that form β-sheets and the subsequent self-assembled structures emerged in the past decades....
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