Silk–elastinlike protein polymer hydrogels: Influence of monomer sequence on physicochemical properties

Dandu, Ramesh; Cresce, Arthur v.; Briber, Robert M.; Dowell, Paul; Cappello, Joseph; Ghandehari, Hamidreza

doi:10.1016/j.polymer.2008.11.047

Cited by 68 publications

(101 citation statements)

References 23 publications

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“…Silk-elastin-like peptide polymer (SELP) was produced using genetic modifications described by Dandu et al [38]. One SELP unit consisted of 8 Bombyx mori silk-like (GAGAGS), 15 elastin-like(GVGVP), and one lysine-modified elastin-like (GKGVP) blocks.…”

Section: Experimental Methodsmentioning

confidence: 99%

“…A model amyloid peptide that has recently drawn much attention is silk-elastin-like peptide polymer (SELP) [38,39]. It consists of alternating domains of 8 silk-like units (GAGAGS), 15 elastin-like units (GVGVP), and 1 elastin unit modified by the substitution of valine for lysine (GKGVP) [38].…”

Section: Silk-elastin-like Peptide (Selp)mentioning

confidence: 99%

“…It consists of alternating domains of 8 silk-like units (GAGAGS), 15 elastin-like units (GVGVP), and 1 elastin unit modified by the substitution of valine for lysine (GKGVP) [38]. The elastin unit provides its thermoresponsive property and the silk unit controls the stiffness of the hydrogel which SELP forms near body temperature.…”

Section: Silk-elastin-like Peptide (Selp)mentioning

confidence: 99%

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Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

et al. 2013

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Self-assembly of amyloid nanofiber is associated with functional and pathological processes such as in neurodegenerative diseases. Despite intensive studies, stochastic nature of the process has made it difficult to elucidate molecular mechanisms for the key amyloid nucleation. Here, we investigated the amyloid nucleation of silk-elastinlike peptide (SELP) using time-lapse lateral force microscopy (LFM). By repeated scanning a single line on a SELP-coated mica surface, we observed sudden stepwise height increases, corresponds to nucleation of an amyloid fiber. The lateral force profiles followed either a worm-like chain model or an exponential function, suggesting that the atomic force microscopy (AFM) tip stretches a single or multiple SELP molecules along the scanning direction, serves as the template for further selfassembly perpendicular to the scan direction. Such mechanically induced nucleation of amyloid fibrils allows positional and directional control of amyloid assembly in vitro, which we demonstrate by generating single nanofibers at predetermined nucleation sites.

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Section: Experimental Methodsmentioning

confidence: 99%

Section: Silk-elastin-like Peptide (Selp)mentioning

confidence: 99%

Section: Silk-elastin-like Peptide (Selp)mentioning

confidence: 99%

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Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

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“…The selection of the structural domain is further dependent on the intended application, for example, elastinlike polypeptides (ELPs) and silklike polypeptides are used for their thermal responsiveness and material strength, respectively [23,24]. One or more substitutions to the primary structure of the polypeptide chain have a direct effect on the physical and chemical properties of the protein-engineered hydrogel [25]. As such, novel amino acid sequences can be rationally designed to modulate structural behavior and function.…”

Section: Design Of Protein-engineered Hydrogelsmentioning

confidence: 99%

Hydrogels from Protein Engineering

Greenwood‐Goodwin

Heilshorn

2012

Biomimetic Approaches for Biomaterials Development

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Protein-engineered hydrogels build upon the natural structure and function of proteins to create well-defined, multifunctional materials by cross-linking polypeptide chains together. Individual polypeptide chains are composed of independent peptide domains built from amino acid monomers. The engineered amino acid sequence is designed to form specific and reproducible structures of the selected peptide domains. The exact amino acid sequence of the polypeptide chain can be encoded into a DNA sequence, which is transfected into a host microorganism in order to produce a monodisperse batch of polypeptide chains. Interactions between individual polypeptide chains can be engineered to form hydrated macromolecular structures with tunable mechanical strength. These interchain interactions can include both noncovalent cross-linking between neighboring peptide domains as well as covalent cross-linking between amino acid residues to form stable hydrogels.In this chapter, we discuss the development of protein-engineered hydrogels with tunable mechanical and biochemical properties for biomaterial applications. First, we discuss the fundamentals of protein structure and recombinant protein synthesis. Next, we review the diversity of peptide domains that have been utilized in protein-engineered hydrogels to date, including cell-binding domains, structural domains, and molecular recognition domains. We continue to describe the various enzymatic and synthetic chemistry strategies that have been utilized to create covalently cross-linked protein-engineered hydrogels. We conclude with an in-depth discussion of cellular interactions with protein-engineered hydrogels and of the ability to tune the biomechanics and biochemistry of the materials to direct cellular phenotype.Development of novel protein-engineered hydrogels for therapeutic applications requires regulation of specific cellular behavior through tuning of the structural, mechanical, and biochemical properties of the hydrogel. The cellular response and activation of intracellular signaling pathways for cell adhesion and migration is different between traditional two-dimensional (2D) cell culture environments and native three-dimensional (3D) cell environments, thus the use of 3D materials for Biomimetic Approaches for Biomaterials Development, First Edition. Edited by João F. Mano.

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“…4 Likely, large amino acid chains provide a rich source of structural/functional variability and complexity. Herein, two SELP polymers, SELP-47 K (MW: 69,814 theoretical calculation 5 and 69 699 mass spectroscopy 6 ) and SELP-815 K (MW: 65 374 theoretical calculation 7 ), are used as a model system to study self-assembly of high molecular-weight proteins. The complete amino acid sequences of SELP-47K and SELP-815 K are MDPVVLQRRDWENPGVTQLNRLAAHPPFASDPMGAG SGAGAGS[(GVGVP) 4 GKGVP(GVGVP) 3 (GAGAGS) 4 ] 12 (GVGVP) 4 GKGVP(GVGVP) 3 (GAGAGS) 2 GAGAMDPGR YQDLRSHHHHHH (one letter amino-acid abbreviation is used) 5 and MDPVVLQRRDWENPGVTQLNRLAAHPPF ASDPM[GAGS(GAGAGS) 2 (GVGVP) 4 GKGVP(GVGV P) 11 (GAGAGS) 4 GAGA] 6 MDPGRYQDLRSHHHHHH, respectively.…”

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confidence: 99%

Ordering recombinant silk-elastin-like nanofibers on the microscale

Zeng

Teng

Jiang

et al. 2014

Applied Physics Letters

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Self-assembled peptide/polypeptide nanofibers are appealing building blocks for creating complex three-dimensional structures. However, ordering assembled peptide/polypeptide nanofibers into three-dimensional structures on the microscale remains challenging and often requires the employment of top-down approaches. We report that silk-elastin-like protein polymers selfassemble into nanofibers in physiologically relevant conditions, the assembled nanofibers further form fiber clusters on the microscale, and the nanofiber clusters eventually coalesce into threedimensional structures with distinct nanoscale and microscale features. It is believed that the interplay between fiber growth and molecular diffusion leads to the ordering of the assembled silk-elastin-like nanofibers at the microscale. V C 2014 AIP Publishing LLC.[http://dx.doi.org/10.1063/1.4863077] Self-assembled peptide/protein nanostructures may find important applications in various areas, including tissue engineering, biosensors, and drug delivery. As an example, self-assembled peptide nanofibers enable the cells to interact with the matrix in three-dimensional microenvironments, enhancing neurite outgrowth. 1 However, it remains a daunting challenge to order self-assembled peptide nanofibers into three-dimensional structures on the microscale. It has been suggested to integrate top-down approaches and selfassembly in the fabrication of microscale-ordered nanostructures. 2 Nevertheless, this strategy not only requires additional capital investment in fabrication facilities but also comprises the elegance of molecular self-assembly, including ease of processing and energy efficiency. Here, we report that, driven by the interplay of fiber nucleation/growth with molecular diffusion, silk-elastin-like protein (SELP) polymers self-assemble into three-dimensional structures with distinct nanoscale and microscale features.Owing to relative ease of design, synthesis, and purification, most self-assembling peptides that have been extensively explored are small peptides, containing several to a few tens of amino acids. 3 In contrast, living systems often utilize high molecular-weight proteins, such as actin and collagen, as building blocks to create nanofiber-based intracellular and extracellular matrices. 4 Likely, large amino acid chains provide a rich source of structural/functional variability and complexity. Herein, two SELP polymers, SELP-47 K (MW: 69,814 theoretical calculation 5 and 69 699 mass spectroscopy 6 ) and SELP-815 K (MW: 65 374 theoretical calculation 7 ), are used as a model system to study self-assembly of high molecular-weight proteins. The complete amino acid sequences of SELP-47K and SELP-815 K are MDPVVLQRRDWENPGVTQLNRLAAHPPFASDPMGAG SGAGAGS[(GVGVP) 4 GKGVP(GVGVP) 3 (GAGAGS) 4 ] 12 (GVGVP) 4 GKGVP(GVGVP) 3 (GAGAGS) 2 GAGAMDPGR YQDLRSHHHHHH (one letter amino-acid abbreviation is used) 5 and MDPVVLQRRDWENPGVTQLNRLAAHPPF ASDPM[GAGS(GAGAGS) 2 (GVGVP) 4 GKGVP(GVGV P) 11 (GAGAGS) 4 GAGA] 6 MDPGRYQDLRSHHHHHH, respectively. 6 In the design of SE...

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Silk–elastinlike protein polymer hydrogels: Influence of monomer sequence on physicochemical properties

Cited by 68 publications

References 23 publications

Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

Hydrogels from Protein Engineering

Ordering recombinant silk-elastin-like nanofibers on the microscale

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