Assessing Cellular Response to Functionalized α‐Helical Peptide Hydrogels

Mehrban, Nazia; Abelardo, Edgardo; Wasmuth, Alexandra; Hudson, Kieran L.; Mullen, Leanne; Thomson, Andrew; Birchall, Martin A.; Woolfson, Derek N.

doi:10.1002/adhm.201400065

Cited by 41 publications

(41 citation statements)

References 41 publications

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“…To circumvent this, specific residues in the sixth position of the heptad can be substituted with synthetic amino acids bearing azido and allyl moieties, without compromising their propensity to self‐assemble . Post‐assembly, cell adhesion ligands such as RGDS can be appended by copper(I)‐catalyzed azide‐alkyne and thiol‐ene click reactions . Such bioorthogonal dual functionalization will enables the presentation of two different ligands independently to influence cell fate.…”

Section: Short Peptides That Self‐assemble Into Biomimetic Hydrogel Smentioning

confidence: 99%

“…Such bioorthogonal dual functionalization will enables the presentation of two different ligands independently to influence cell fate. While undecorated hSAF hydrogels support support neuronal cell growth and neurite extension,[147a] scaffolds functionalized with RGDS demonstrated greater cell adhesion, proliferation and differentiation of precursor cells …”

Section: Short Peptides That Self‐assemble Into Biomimetic Hydrogel Smentioning

confidence: 99%

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Self‐Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration

Loo

Göktas

Tekinay

et al. 2015

Adv Healthcare Materials

124

123

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and their complex biological functions closely link to their high order organization; therefore such scaffolds need to mimic the hierarchical structure of natural tissues in order to provide the necessary structural and biomechanical framework. Furthermore, biomimetic scaffolds need to display the necessary biochemical and signaling cues for cellular function. The native ECM provides structural support and instructive cues to cells through the macromolecules found in its structure such as proteins, glycosaminoglycans and polysaccharides. ECM macromolecules contain bioactive signal sequences that are recognized by cells via cell transmembrane receptors called integrins. Interaction between integrins and bioactive epitopes of ECM activates signal transduction mechanisms, which can induce specifi c cellular functions including adhesion, migration, proliferation and differentiation. Such bioactive epitopes include: the RGD adhesive sequence found in the structure of ECM proteins such as fi bronectin and vitronectin, [ 1 ] the IKVAV peptide sequence from laminin known to induce neural attachment, migration and neurite outgrowth; [ 2 ] and the YIGSR peptide sequence derived from the laminin β-chain. [ 3 ] Moreover, the native ECM provides to cells a highly dynamic complex microenvironment that enables cell motility and time-varying display of bioactive cues via continuous matrix remodeling. In natural cellular microenvironment, ECM is constantly degraded by proteases and remodeled by proteins secreted from cells. Mimicking the ECM can therefore be the best strategy to develop advanced functional materials to control cellular behavior and Self-assembling proteins and peptides are increasingly gaining interest for potential use as scaffolds in tissue engineering applications. They selforganize from basic building blocks under mild conditions into supramolecular structures, mimicking the native extracellular matrix. Their properties can be easily tuned through changes at the sequence level. Moreover, they can be produced in suffi cient quantities with chemical synthesis or recombinant technologies to allow them to address homogeneity and standardization issues required for applications. Here. recent advances in self-assembling proteins, peptides, and peptide amphiphiles that form scaffolds suitable for tissue engineering are reviewed. The focus is on a variety of motifs, ranging from minimalistic dipeptides, simplistic ultrashort aliphatic peptides, and peptide amphiphiles to large "recombinamer" proteins. Special emphasis is placed on the rational design of self-assembling motifs and biofunctionalization strategies to infl uence cell behavior and modulate scaffold stability. Perspectives for combination of these "bottom-up" designer strategies with traditional "top-down" biofabrication techniques for new generations of tissue engineering scaffolds are highlighted.

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Section: Short Peptides That Self‐assemble Into Biomimetic Hydrogel Smentioning

confidence: 99%

Section: Short Peptides That Self‐assemble Into Biomimetic Hydrogel Smentioning

confidence: 99%

Self‐Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration

Loo

Göktas

Tekinay

et al. 2015

Adv Healthcare Materials

124

123

View full text Add to dashboard Cite

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“…Panel (a) reprinted with permission from Banwell et al 3 Copyright 2009 Macmillan Publishers Ltd. Panels (b) reprinted with permission from Mehrban et al 43 Copyright 2014 Wiley–VCH Verlag GmbH & Co.…”

Section: Figurementioning

confidence: 99%

The Powerful Functions of Peptide-Based Bioactive Matrices for Regenerative Medicine

et al. 2014

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In an effort to develop bioactive matrices for regenerative medicine, peptides have been used widely to promote interactions with cells and elicit desired behaviors in vivo. This paper describes strategies that utilize peptide-based molecules as building blocks to create supramolecular nanostructures that emulate not only the architecture but also the chemistry of the extracellular matrix in mammalian biology. After initiating a desired regenerative response in vivo, the innate biodegradability of these systems allow for the natural biological processes to take over in order to promote formation of a new tissue without leaving a trace of the nonnatural components. These bioactive matrices can either bind or mimic growth factors or other protein ligands to elicit a cellular response, promote specific mechanobiological responses, and also guide the migration of cells with programmed directionality. In vivo applications discussed in this review using peptide-based matrices include the regeneration of axons after spinal cord injury, regeneration of bone, and the formation of blood vessels in ischemic muscle as a therapy in peripheral arterial disease and cardiovascular diseases.

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“…The resulting peptides could be functionalized with a variety of functional peptides using copper‐catalyzed azide‐alkyne click chemistry, yielding up to 100% conjugation. This approach was used to conjugate an RGDS cell‐adhesion motif onto a coiled‐coil fiber hydrogel for the culture of PC 12 cells and enables the introduction of considerably diverse functionality …”

Section: Coiled‐coil Peptide Nanofiber Decoration For Biological Applmentioning

confidence: 99%

α‐Helical coiled‐coil peptide materials for biomedical applications

Collier

2016

WIREs Nanomed Nanobiotechnol

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Self-assembling coiled coils, which occur commonly in native proteins, have received significant interest for the design of new biomaterials-based medical therapies. Considerable effort over recent years has led to a detailed understanding of the self-assembly process of coiled coils, and a diverse collection of strategies have been developed for designing functional materials using this motif. The ability to engineer the interface between coiled coils allows one to achieve variously connected components, leading to precisely defined structures such as nanofibers, nanotubes, nanoparticles, networks, gels, and combinations of these. Currently these materials are being developed for a range of biotechnological and medical applications, including drug delivery systems for controlled release, targeted nanomaterials, “drug-free” therapeutics, vaccine delivery systems, and others.

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Assessing Cellular Response to Functionalized α‐Helical Peptide Hydrogels

Cited by 41 publications

References 41 publications

Self‐Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration

Self‐Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration

The Powerful Functions of Peptide-Based Bioactive Matrices for Regenerative Medicine

α‐Helical coiled‐coil peptide materials for biomedical applications

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