Double‐hydrophobic elastin‐like polypeptides with added functional motifs: Self‐assembly and cytocompatibility

Le, Duc Anh; Tsutsui, Yoko; Sugawara‐Narutaki, Ayae; Yukawa, Hiroshi; Baba, Yoshinobu; Ohtsuki, Chikara

doi:10.1002/jbm.a.36105

Cited by 16 publications

(31 citation statements)

References 52 publications

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“…The spectrum of GPG noticeably changed with time at 37 • C; the intensity of the negative band seen at around 220 nm continuously increased over the course of seven days with slight blue shifts [28,29]. In addition, the band observed at around 200 nm became positive after one day, and its intensity increased with time.…”

Section: Self-assembly Of Gpg and Gppgmentioning

confidence: 96%

“…Our group has developed a novel class of "double-hydrophobic" ELP block copolymers, named GPG [28][29][30][31][32], which was inspired by the non-homogeneous distribution of glycine-rich and proline-rich hydrophobic domains in monomer elastin [33]. GPG contains the basic sequence (VGGVG) 5 -(VPGXG) 25 -(VGGVG) 5 , where X is V (80%) or F (20%) (F: Phe) to tune the T t at around room temperature ( Figure 1).…”

Section: Introductionmentioning

confidence: 99%

“…The glycine-rich (VGGVG) 5 and the proline-rich (VPGXG) 25 both dehydrate at higher temperatures; however, they form distinct secondary structures, namely, β-sheet and β-turn structures, respectively. In water above 37 • C, GPG initially assembles to form nanoparticles that are rich in β-turn structures that connect to generate beaded nanofibers with the formation of β-sheet structures between the nanoparticles [28,29,32]. The distinguishing feature of GPG over conventional ELPs is that the nanofibers are obtained as a stable colloidal dispersion without forming precipitates; therefore, they can be easily coated on substrates through the drying process [29].…”

Section: Introductionmentioning

confidence: 99%

“…In water above 37 • C, GPG initially assembles to form nanoparticles that are rich in β-turn structures that connect to generate beaded nanofibers with the formation of β-sheet structures between the nanoparticles [28,29,32]. The distinguishing feature of GPG over conventional ELPs is that the nanofibers are obtained as a stable colloidal dispersion without forming precipitates; therefore, they can be easily coated on substrates through the drying process [29]. Furthermore, various functional amino acid motifs, including crosslinkable [30], cell binding [29], and silver binding [31] sequences, can be fused to the C-terminus of GPG without hampering its fiber-forming abilities, thus demonstrating the robust self-assembling characteristics of this block sequence.…”

Section: Introductionmentioning

confidence: 99%

“…The distinguishing feature of GPG over conventional ELPs is that the nanofibers are obtained as a stable colloidal dispersion without forming precipitates; therefore, they can be easily coated on substrates through the drying process [29]. Furthermore, various functional amino acid motifs, including crosslinkable [30], cell binding [29], and silver binding [31] sequences, can be fused to the C-terminus of GPG without hampering its fiber-forming abilities, thus demonstrating the robust self-assembling characteristics of this block sequence. However, it has never been clarified whether the block length exerted influence on the self-assembly of this double-hydrophobic polypeptide, despite the fact that the block length is an important parameter in the self-assembly processes of block copolymers [19,25,34].…”

Section: Introductionmentioning

confidence: 99%

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Rheology of Dispersions of High-Aspect-Ratio Nanofibers Assembled from Elastin-Like Double-Hydrophobic Polypeptides

Sugawara‐Narutaki

Yasunaga

Sugioka

et al. 2019

IJMS

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Elastin-like polypeptides (ELPs) are promising candidates for fabricating tissue-engineering scaffolds that mimic the extracellular environment of elastic tissues. We have developed a “double-hydrophobic” block ELP, GPG, inspired by non-uniform distribution of two different hydrophobic domains in natural elastin. GPG has a block sequence of (VGGVG)5-(VPGXG)25-(VGGVG)5 that self-assembles to form nanofibers in water. Functional derivatives of GPG with appended amino acid motifs can also form nanofibers, a display of the block sequence’s robust self-assembling properties. However, how the block length affects fiber formation has never been clarified. This study focuses on the synthesis and characterization of a novel ELP, GPPG, in which the central sequence (VPGVG)25 is repeated twice by a short linker sequence. The self-assembly behavior and the resultant nanostructures of GPG and GPPG were when compared through circular dichroism spectroscopy, atomic force microscopy, and transmission electron microscopy. Dynamic rheology measurements revealed that the nanofiber dispersions of both GPG and GPPG at an extremely low concentration (0.034 wt%) exhibited solid-like behavior with storage modulus G′ > loss modulus G” over wide range of angular frequencies, which was most probably due to the high aspect ratio of the nanofibers that leads to the flocculation of nanofibers in the dispersion.

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Section: Self-assembly Of Gpg and Gppgmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Rheology of Dispersions of High-Aspect-Ratio Nanofibers Assembled from Elastin-Like Double-Hydrophobic Polypeptides

Sugawara‐Narutaki

Yasunaga

Sugioka

et al. 2019

IJMS

Self Cite

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Elastin‐Like Recombinamers: Deconstructing and Recapitulating the Functionality of Extracellular Matrix Proteins Using Recombinant Protein Polymers

Acosta

Quintanilla‐Sierra

Mbundi

et al. 2020

Adv Funct Materials

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In the development of tissue engineering strategies to replace, remodel, regenerate, or support damaged tissue, the development of bioinspired biomaterials that recapitulate the physicochemical characteristics of the extracellular matrix has received increased attention. Given the compositional heterogeneity and tissue-to-tissue variation of the extracellular matrix, the design, choice of polymer, crosslinking, and nature of the resulting biomaterials are normally depended on intended application. Generally, these biomaterials are usually made of degradable or nondegradable biomaterials that can be used as cell or drug carriers. In recent years, efforts to endow reciprocal biomaterial-cell interaction properties in scaffolds have inspired controlled synthesis, derivatization, and functionalization of the polymers used. In this regard, elastin-like recombinant proteins have generated interest and continue to be developed further owing to their modular design at a molecular level. In this review, the authors provide a summary of key extracellular matrix features relevant to biomaterials design and discuss current approaches in the development of extracellular matrix-inspired elastin-like recombinant protein based biomaterials.

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Gelatin Templated Polypeptide Co‐Cross‐Linked Hydrogel for Bone Regeneration

Qiao

Liu

Zhou

et al. 2019

Adv Healthcare Materials

125

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Polypeptides with short chains of amino acid monomers have been widely applied in the clinic because of their various biological functions. However, the easily‐inactivated characteristics and burst releasing of the peptides limit their application in vivo. Here, a novel osteogenic polypeptide hydrogel (GelMA‐c‐OGP) is created by co‐cross‐linking template photo‐cross‐linked gelatin (GelMA) with photo‐cross‐linkable osteogenic growth peptides (OGP) using ultraviolet radiation. GelMA enables the formation of hydrogel with photo‐cross‐linkable OGP with good mechanical properties and also promotes bone regeneration. GelMA‐c‐OGP hydrogel accelerates the bone formation procedure of osteogenic precursor cells by significantly enhancing the expression of osteogenic‐related genes BMP‐2, OCN, and OPN, and increasing the precipitation of calcium salts in osteoblasts. Similarly, GelMA‐c‐OGP hydrogel promotes bone regeneration in vivo. Furthermore, it is observed that more collagen fibers connect cortical bones in the GelMA‐c‐OGP implanted group than the control group by hematoxylin‐eosin and immunohistochemical staining of Collagen I and TGF‐β. The co‐cross‐linked OGP polypeptide converts from liquid to solid hydrogel with transient UV light in situ, which also can strengthen the mechanical property of the defect bone and avoid burst osteogenic peptide, releasing during the bone defect healing period. Overall, this hydrogel delivering system has a significant impact on bone defect healing compared with traditional methods.

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Double‐hydrophobic elastin‐like polypeptides with added functional motifs: Self‐assembly and cytocompatibility

Cited by 16 publications

References 52 publications

Rheology of Dispersions of High-Aspect-Ratio Nanofibers Assembled from Elastin-Like Double-Hydrophobic Polypeptides

Rheology of Dispersions of High-Aspect-Ratio Nanofibers Assembled from Elastin-Like Double-Hydrophobic Polypeptides

Elastin‐Like Recombinamers: Deconstructing and Recapitulating the Functionality of Extracellular Matrix Proteins Using Recombinant Protein Polymers

Gelatin Templated Polypeptide Co‐Cross‐Linked Hydrogel for Bone Regeneration

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