Genetic Engineering of Stimuli-Sensitive Silkelastin-like Protein Block Copolymers

Nagarsekar, Ashish; Crissman, John; Crissman, Mary; Ferrari, Franco; Cappello, Joseph; Ghandehari, Hamidreza

doi:10.1021/bm0201082

Cited by 93 publications

(95 citation statements)

References 27 publications

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“…Stimuliresponsive silk-elastin polymers can be prepared since T t decreases with increasing polymer length, polymer concentration and ionic strength. By replacing a Val by Glu, T t also responds to pH (until pH 7.0) [176]. Block composition and polymer length are of major importance for mechanical properties, biodegradability (which is primarily by enzymatic hydrolysis) and physiological properties of these proteins.…”

Section: Hybrids Of Elastin With Other Moleculesmentioning

confidence: 99%

Elastin as a biomaterial for tissue engineering

et al. 2007

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Section: Hybrids Of Elastin With Other Moleculesmentioning

confidence: 99%

Elastin as a biomaterial for tissue engineering

et al. 2007

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“…These hydrogels spontaneously crosslink and quickly form a gel in vivo following injection at the site. Self-assembling hydrogels can also incorporate a number of stimuli such as temperature or pH to control the matrix assembly [139,161].…”

Section: Local Delivery-mentioning

confidence: 99%

“…One route to increasing its solubility is the incorporation of peptide sequences from other proteins, such as elastin, that disrupt β-sheet formation [50]. Silk elastin-like polypeptides (SELPs) are chimeric proteins designed to retain the mechanical properties of silk, while incorporating the high solubility and environmental sensitivity of ELPs [139,161,168]. Some SELPs can be injected through hypodermic needles, and they then form insoluble hydrogels at the injection site without chemical assistance [162,[169][170][171].…”

Section: Silk-elp Hybridsmentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

286

231

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Peptides are emerging as a new class of biomaterials due to their unique chemical, physical, and biological properties. The development of peptide-based biomaterials is driven by the convergence of protein engineering and macromolecular self-assembly. This review covers the basic principles, applications, and prospects of peptide-based biomaterials. We focus on both chemically synthesized and genetically encoded peptides, including poly-amino acids, elastin-like polypeptides, silk-like polymers and other biopolymers based on repetitive peptide motifs. Applications of these engineered biomolecules in protein purification, controlled drug delivery, tissue engineering, and biosurface engineering are discussed.

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“…Furthermore, many SELR designs incorporate such a high SL percentage that the contribution of the elastomeric portion to the self-assembly process is imperceptible 27,28 . However, experience with SELR designs with a lower SL content has demonstrated that, in such compositions, the EL blocks are able to maintain their characteristic thermal transition [28][29][30] . One of the main drawbacks associated with the use of SL motifs as physical crosslinking domains to obtain injectable hydrogels is that the kinetics of β-sheet formation under physiological conditions (aqueous medium, neutral pH and 37°C) is too slow 31 .…”

Section: Introductionmentioning

confidence: 99%

Self-Organized ECM-Mimetic Model Based on an Amphiphilic Multiblock Silk-Elastin-Like Corecombinamer with a Concomitant Dual Physical Gelation Process

et al. 2014

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ABSTRACT. Although significant progress has been made in the area of injectable hydrogels for biomedical applications and model cell niches, further improvements are still needed, especially in terms of mechanical performance, stability and biomimicry of the native fibrillar architecture found in the extracellular matrix (ECM). This work focuses on the design and production of a silk-elastin-based injectable multiblock co-recombinamer that spontaneously forms a stable physical nanofibrillar hydrogel under physiological conditions. That differs from previously reported silk-elastin-like polymers on a major content and predominance of the elastin-like part, as well as a more complex structure and behavior of such part of the molecule, which is aimed to obtain well defined hydrogels.Rheological and DSC experiments showed that this system displays a coordinated and concomitant dual gelation mechanism. In a first stage, a rapid, thermally driven gelation of the co-recombinamer solution takes place once the system reaches body temperature due to the thermal responsiveness of the elastinlike (EL) parts and the amphiphilic multiblock design of the co-recombinamer. A bridged micellar 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 2 structure is the dominant microscopic feature of this stage, as demonstrated by AFM and TEM.Completion of the initial stage triggers the second, which comprises a stabilization, reinforcement, and microstructuring of the gel. FTIR analysis shows that these events involve the formation of β-sheets around the silk motifs. The emergence of such β-sheet structures leads to the spontaneous selforganization of the gel into the final fibrous structure. Despite the absence of biological cues, here we set the basis of the minimal structure that is able to display such a set of physical properties and undergo microscopic transformation from a solution to a fibrous hydrogel. The results point to the potential of this system as a basis for the development of injectable fibrillar biomaterial platforms towards a fully functional, biomimetic, artificial extracellular matrix and cell niches.

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Genetic Engineering of Stimuli-Sensitive Silkelastin-like Protein Block Copolymers

Cited by 93 publications

References 27 publications

Elastin as a biomaterial for tissue engineering

Elastin as a biomaterial for tissue engineering

Peptide-based biopolymers in biomedicine and biotechnology

Self-Organized ECM-Mimetic Model Based on an Amphiphilic Multiblock Silk-Elastin-Like Corecombinamer with a Concomitant Dual Physical Gelation Process

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