研究者詳細 - 前田　衣織

論文 - 前田　衣織

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Development of the efficient preparation method for thermoresponsive elastin-like peptides using liquid-phase synthesis combined with fragment condensation strategy 査読有り国際誌

Yoshida K., Suyama K., Matsushita S., Maeda I., Nose T.

J Pept Sci 29 ( 12 ) e3528 2023年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are synthetic peptides that mimic the characteristic hydrophobic amino acid repeat sequences of elastin and exhibit temperature-dependent reversible self-assembly properties. ELPs are expected to be used as temperature-responsive biomolecular materials across diverse industrial and research fields, and there is a requirement for a straightforward method to mass-produce them. Previously, we demonstrated that phenylalanine-containing ELP analogs, namely, (FPGVG)n , can undergo coacervation with short chains (n = 5). The Fmoc solid-phase peptide synthesis method is one strategy used to synthesize these short ELPs. However, owing to its low reaction efficiency, an efficient method for preparing ELPs is required. In this study, efficient preparation of ELPs was investigated using a liquid-phase synthesis method with a hydrophobic benzyl alcohol support (HBA-tag). Because HBA-tags are highly hydrophobic, they can be easily precipitated by the addition of poor solvents and recovered by filtration. This property allows the method to combine the advantages of the simplicity of solid-phase methods and the high reaction efficiency of liquid-phase methods. By utilizing liquid-phase fragment condensation with HBA-tags, short ELPs were successfully obtained in high yield and purity. Finally, the temperature-dependent response of the ELPs generated through fragment condensation was assessed using turbidity measurements, which revealed a reversible phase transition. Consequently, the ELPs exhibited a reversible phase transition, indicating successful synthesis of ELPs via fragment preparation with tags. These findings provide evidence of the potential for mass production of ELPs using this approach.

DOI： 10.1002/psc.3528

その他リンク： https://pubmed.ncbi.nlm.nih.gov/37340996/

Enhancement of Aggregate Formation Through Aromatic Compound Adsorption in Elastin-like Peptide (FPGVG)<inf>5</inf> Analogs 査読有り

Suyama K., Murashima M., Maeda I., Nose T.

Biomacromolecules 24 ( 11 ) 5265 - 5276 2023年11月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) exhibit temperature-dependent reversible self-assembly. Repetitive sequences derived from elastin, such as Val-Pro-Gly-Val-Gly (VPGVG), are essential for the self-assembly of ELPs. Previously, we developed (FPGVG)5 (F5), in which the first valine residue in the VPGVG sequence was replaced with phenylalanine, which showed strong self-aggregation ability. This suggests that interactions through the aromatic amino acid residues of ELPs could play an important role in self-assembly. In this study, we investigated the thermoresponsive behavior of F5 analogs in the presence of aromatic compounds. Turbidimetry, spectroscopy, and fluorescence measurements demonstrated that aromatic compounds interacted with F5 analogs below the transition temperature and enhanced the self-assembly ability of ELPs by stabilizing amyloid-like structures. Furthermore, quantitative high-performance liquid chromatography analyses showed that the F5 analogs could adsorb and remove hydrophobic aromatic compounds from aqueous solutions during aggregate formation. These results suggested that the F5 analogs can be applicable as scavengers of aromatic compounds.

DOI： 10.1021/acs.bio mac.3c00779

その他リンク： https://pubmed.ncbi.nlm.nih.gov/37865930/

Determining the Sequence Dependency of Self-Assembly of Elastin-Like Peptides Using Short Peptide Analogues with Shuffled Repetitive Sequences 査読有り国際誌

Tatsubo D., Suyama K., Sakamoto N., Tomohara K., Taniguchi S., Maeda I., Nose T.

Biochemistry 62 ( 17 ) 2559 - 2570 2023年09月

記述言語：英語掲載種別：研究論文（学術雑誌）

Synthetic elastin-like peptides (ELPs) that possess characteristic tropoelastin-derived hydrophobic repetitive sequences, such as (VPGVG)n, exhibit thermoresponsive reversible self-assembly. Although their thermoresponsive properties have been well-studied, the sequence-dependent and structural requirements for self-assembly remain ambiguous. In particular, it is still unclear whether the amino acid sequences derived from tropoelastin are necessary for self-assembly. In this study, 11 sequence-shuffled ELP analogues based on (FPGVG)5, which is a previously developed short ELP (sELP), were designed to elucidate the sequence-dependent and structural requirements for their self-assembly. Among them, eight shuffled peptides exhibited self-assembling properties, whereas the other three peptides were difficult to dissolve in water. Structural analyses revealed that the structural characteristics of the three insoluble peptides were different from those of their thermoresponsive analogues. Furthermore, the secondary structures of the peptide analogues possessing the self-assembly abilities were different from each other. These results suggest that the potential for self-assembly and water solubility of sELPs depend on the primary structure in each repeated unit. Moreover, several shuffled analogues exhibited more potent self-assembling properties than the original (FPGVG)5, indicating that shorter ELPs can be obtained using their novel motifs as repetitive units. We also observed that the presence of Pro-Gly sequence in the repeating units was advantageous in terms of peptide solubility. Although further analysis will be necessary to elucidate the molecular mechanism underlying the self-assembly of these sELPs, this study provides insights into the relationship between the amino acid sequence and the self-assembling ability of the peptides for developing new sELPs for various applications.

DOI： 10.1021/acs.biochem.3c00146

その他リンク： https://pubs.acs.org/doi/10.1021/acs.biochem.3c00146

Aromatic compounds scavenging ability of thermo-responsive short elastin-like peptide (FPGVG)n analogs 査読有り国際誌

Keitaro Suyama ,Masayuki Murashima,Iori Maeda ,Takeru Nose

Peptide Science 2022 ( 日本ペプチド学会 ) 25 - 26 2023年03月

Branched short elastin-like peptides with temperature responsiveness obtained by EDTA-mediated multimerization 査読有り国際誌

Tanaka N., Suyama K., Tomohara K., Maeda I., Nose T.

J Pept Sci 29 ( 2 ) e3449 p.1-10 2023年02月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) exhibit a reversible phase transition, known as coacerva- tion, triggered by temperature changes. This property makes them useful as stimuli- responsive molecular materials for various applications. Among ELPs, short peptide chain lengths have some advantages over long peptide chain lengths because short ELPs can be easily obtained by chemical synthesis, allowing the use of various amino acids, including D-type and unnatural amino acids, at any position in the sequence. Moreover, the incorporated amino acids readily affect the temperature-responsive behavior of ELPs. However, to be utilized in various applications, it is necessary to develop short ELPs and to investigate their temperature-responsive properties. To obtain further insights into the temperature-responsive behavior of the short ELPs, we investigated branched short ELP analogs composed of (FPGVG)n chains (n = 1 or 2, abbreviated as F1 and F2, respectively). We synthesized multimers composed of four F1 chains or two to four F2 chains using ethylenediaminetetraacetic acid (EDTA) as a central component of multimerization. Our results show that the multimers obtained exhibited coacervation in aqueous solutions whereas linear F1 or F2 did not. Furthermore, the structural features of the obtained multimers were the same as those of linear (FPGVG)4. In this study, we demonstrated that molecules capable of coacervation can be obtained by multimerization of F1 or F2. The temperature- responsive molecules obtained using short ELPs make it possible to use them as easy-to-synthesize peptide tags to confer temperature responsiveness to various molecules, which will aid the development of temperature-responsive biomaterials with a wide variety of functions.

DOI： 10.1002/psc.3449

その他リンク： https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3449

Suitability of high-molecular-weight tissue-derived elastin polypeptides and their particles as cosmetic biomaterials 査読有り国際誌

Sakai T., Sodemoto N., Inoue A., Taniguchi S., Maeda I., Hikima T.

J Pept Sci e3472 p.1-10 2022年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

We aimed to determine the coacervation properties of high-molecular-weight (HMW) tissue-derived elastin (TDE) and to examine the potential use of TDE parti- cles as a cosmetic biomaterial. TDE solutions were filtered and divided into three fractions (1–3) according to the molecular weight of the elastin. The turbidity of frac- tion 2, which contained a large portion (58%) of HMW elastin polypeptides (>100 kDa), was measured under several pH values (3.0–11.0) and NaCl concentra- tions (0–1000 mM) to examine its coacervation ability. HMW TDE exhibited coacer- vation under the physiological conditions (temperature, pH, and NaCl concentration) of the skin surface. We performed inclusion and release experiments using three model chemicals with different molecular weights and measured the size and zeta potential of the fraction 3 particles to investigate the suitability of HMW elastin poly- peptides. Fraction 3, which contained a larger portion (64%) of HMW elastin poly- peptides, displayed a strong coacervation property at a phase transition temperature of 19.8 ± 0.1C. The inclusion ratio of the model chemical Biebrich Scarlet (BS) with a molecular weight of <600 was approximately 92.1 ± 0.7%. The release profiles of BS from the particles linearly increased and reached a plateau after 15 days. Moreover, the average size of the particles with BS was 474.2 ± 24.6 nm. The low-molecular- weight (LMW) elastin peptides have moisturizing and whitening functions for the skin. We concluded that TDE, as a mixture of HMW polypeptides and LMW pep- tides, can potentially serve as a multifunctional and effective cosmetic biomaterial.

DOI： 10.1002/psc.3472

その他リンク： https://pubmed.ncbi.nlm.nih.gov/36541737/

Development of truncated elastin-like peptide analogues with improved temperature-response and self-assembling properties 査読有り

Sumiyoshi S., Suyama K., Tanaka N., Andoh T., Nagata A., Tomohara K., Taniguchi S., Maeda I., Nose T.

Scientific Reports 12 ( 1 ) 2022年11月

記述言語：英語掲載種別：研究論文（学術雑誌）

Functional peptides, which are composed of proteinogenic natural amino acids, are expected to be used as biomaterials with minimal environmental impact. Synthesizing a functional peptide with a shorter amino acid sequence while retaining its function is a easy and economical strategy. Furthermore, shortening functional peptides helps to elucidate the mechanism of their functional core region. Truncated elastin-like peptides (ELPs) are peptides consisting of repetitive sequences, derived from the elastic protein tropoelastin, that show the thermosensitive formation of coacervates. In this study, to obtain shortened ELP analogues, we synthesized several (Phe-Pro-Gly-Val-Gly)n (FPGVG)n analogues with one or two amino acid residues deleted from each repeat sequence, such as the peptide analogues consisting of FPGV and/or FPG sequences. Among the novel truncated ELP analogues, the 16-mer (FPGV)4 exhibited a stronger coacervation ability than the 25-mer (FPGVG)5. These results indicated that the coacervation ability of truncated ELPs was affected by the amino acid sequence and not by the peptide chain length. Based on this finding, we prepared Cd2+-binding sequence-conjugated ELP analogue, AADAAC-(FPGV)4, and found that it could capture Cd2+. These results indicated that the 16-mer (FPGV)4 only composed of proteinogenic amino acids could be a new biomaterial with low environmental impact.

DOI： 10.1038/s41598-022-23940-0

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85141734638&origin=inward

Flexible customization of the self-assembling abilities of short elastin-like peptide Fn analogs by substituting N-terminal amino acids 査読有り国際誌

Suyama K., shimizu M., Maeda I., Nose T.

Biopolymers 113 ( 10 ) e23521 p.1-14 2022年10月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are thermoresponsive biopolymers inspired by the characteristic repetitive sequences of natural elastin. As ELPs exhibit temperature-dependent reversible self-assembly, they are expected to be biocompatible thermoresponsive materials for drug delivery carriers. One of the most widely studied ELPs in this field is the repetitive pentapeptide, (VPGXG)n . We previously reported that phenylalanine-containing ELP (Fn) analogs, in which the former Val residue of the repetitive sequence (VPGVG)n is replaced by Phe, show coacervation with a short chain length (n = 5). Owing to their short sequences, Fn analogs are easily modified in amino acid sequences via simple chemical synthesis, and are useful for investigating the relationship between peptide sequences and temperature responsiveness. In this study, we developed Fn analogs by replacing Phe residue(s) with other amino acids or introducing another amino acid at the N-terminus. The temperature responsiveness of the Fn analogs changed drastically with the substitution of a single Phe residue, suggesting that aromatic amino acids play an important role in their self-assembly. In addition, the self-assembling ability of Fn was enhanced by increasing the bulkiness of the N-terminal amino acids. Therefore, the N-terminal residue was considered to be important for hydrophobicity-induced intermolecular interactions between the peptides during coacervation.

DOI： 10.1002/bip.23521

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85104330108&origin=inward

Development of temperature-responsive peptides by EDTA-mediated multimerization of short (FPGVG)n chains 査読有り国際誌

Naoki Tanaka, Keitaro Suyama, Keisuke Tomohara, Iori Maeda, and Takeru Nose

Peptide Science 2021 ( 日本ペプチド学会 ) 83 - 84 2022年03月

Development of temperature-responsive short-chain peptide analogues based on elastin-like peptide FPGVG 査読有り国際誌

Keitaro Suyama ,Marin Shimizu ,Iori Maeda ,Takeru Nose

Peptide Science 2021 ( 日本ペプチド学会 ) 141 - 142 2022年03月

Metal ion scavenging activity of elastin-like peptide analogues containing a cadmium ion binding sequence 査読有り国際誌

Shogo Sumiyoshi,Keitaro Suyama,Daiki Tatsubo,Naoki Tanaka,Keisuke Tomohara,Suguru Taniguchi,Iori Maeda,Takeru Nose

Scientific Reports ( Nature Publishing group ) 12 ( 1861 ) 1 - 16 1861: Article number 2022年02月

Role of Phe residues in elastin-like peptide (FPGVG)5 on self-assembly properties 査読有り国際誌

Keitaro Suyama ,Marin Shimizu ,Iori Maeda ,Takeru Nose

Peptide Science 2020 ( 日本ペプチド学会 ) 59 - 60 2021年03月

Fractionation of Water-soluble Elastin from Pig Aorta by Coacervation Method 査読有り国際誌

Iori Maeda,Suguru Taniguchi,Yumi Moriuchi,Naruhiko Sawa,Asako Inoue,Tomoyuki Usa,Noriko Watanabe,Keitaro Suyama, Takeru Nose

Peptide Science 2020 ( 日本ペプチド学会 ) 65 - 66 2021年03月

Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG) <inf>n</inf>Using Nitrilotriacetic Acid as a Building Block 査読有り

Suyama K., Mawatari M., Tatsubo D., Maeda I., Nose T.

ACS Omega 6 ( 8 ) 5705 - 5716 2021年03月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin comprises hydrophobic repetitive sequences, such as Val-Pro-Gly-Val-Gly, which are thought to be important for the temperature-dependent reversible self-association (coacervation). Elastin and elastin-like peptides (ELPs), owing to their characteristics, are expected to be applied as base materials for the development of new molecular tools, such as drug-delivery system carrier and metal-scavenging agents. Recently, several studies have been reported on the dendritic or branching ELP analogues. Although the topological difference of the branched ELPs compared to their linear counterparts may lead to useful properties in biomaterials, the available information regarding the effect of branching on molecular architecture and thermoresponsive behavior of ELPs is scarce. To obtain further insight into the thermoresponsive behavior of branched ELPs, novel ELPs, such as nitrilotriacetic acid (NTA)-(FPGVG)n conjugates, that is, (NTA)-Fn analogues possessing 1-3 (FPGVG)n (n = 3, 5) molecule(s), were synthesized and investigated for their coacervation ability. Turbidity measurement of the synthesized peptide analogues revealed that (NTA)-Fn analogues showed strong coacervation ability with various strengths. The transition temperature of NTA-Fn analogues exponentially decreased with increasing number of residues. In the circular dichroism measurements, trimerization did not alter the secondary structure of each peptide chain of the NTA-Fn analogue. In addition, it was also revealed that the NTA-Fn analogue possesses one peptide chain that could be utilized as metal-scavenging agents. The study findings indicated that multimerization of short ELPs via NTA is a useful and powerful strategy to obtain thermoresponsive molecules.

DOI： 10.1021/acsomega.0c06140

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85104330108&origin=inward

Concentration dependent coacervation peoperty of nonlinear elastin-derived peptide (FPGVG)n analogs 査読有り国際誌

Keitaro Suyama,Mika Mawatari,Daiki Tatsubo,Iori Maeda,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 29 - 30 2020年02月

Stability of Phe-containing elastin-like peptides against proteases in digestive organspeptide (FPGVG)n analogs 査読有り国際誌

Iori Maeda,Miki Kawakami,Suguru Taniguchi,Keitaro Suyama,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 161 - 162 2020年02月

Development of liposome-like nanostructures composed of short amphiphilic elastin-like peptidestide (FPGVG)n analogs 査読有り国際誌

Naoki Sakamoto,Daiki Tatsubo,Keiji Sato,Keisuke Tomohara,Keitaro Suyama,Iori Maeda,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 113 - 114 2020年02月

Enhancement of Self-Aggregation Properties of Linear Elastin-Derived Short Peptides by Simple Cyclization: Strong Self-Aggregation Properties of Cyclo[FPGVG]<inf>n</inf>, Consisting only of Natural Amino Acids 査読有り

Suyama K., Tatsubo D., Iwasaki W., Miyazaki M., Kiyota Y., Takahashi I., Maeda I., Nose T.

Biomacromolecules 19 ( 8 ) 3201 - 3211 2018年08月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) consist of distinctive repetitive sequences, such as (VPGVG)n, exhibit temperature-dependent reversible self-assembly (coacervation), and have been considered to be useful for the development of thermoresponsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermoresponsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed their self-assembly properties and structural characteristics. Cyclo[FPGVG]n (n = 3-5) demonstrated stronger coacervation capacity than the corresponding linear peptides. The coacervate of cyclo[FPGVG]5 was able to retain water-soluble dye molecules at 40 °C, which implied that cyclo[FPGVG]5 could be employed as a base material of DDS (drug delivery system) matrices and other biomaterials. The results of molecular dynamics simulations and circular dichroism measurements suggested that a certain chain length was required for cyclo[FPGVG]n to demonstrate alterations in molecular structure that were critical to the exhibition of coacervation.

DOI： 10.1021/acs.biomac.8b00353

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85049214569&origin=inward

Angiotensin I converting enzyme-inhibiting peptides purified from elastase-degraded elastin prepared from pig aorta 査読有り

Maeda I., Kai S., Taniguchi S., Inoue A., Li H., Kesamaru H., Nose T.

Current Enzyme Inhibition 14 ( 1 ) 67 - 74 2018年04月

担当区分：責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Background: Many peptides are produced from food proteins during the manufacturing of various functional foods; unexpected and valuable physiological activities are frequently identified in such released peptides. Elastin, which normally exists as an insoluble elastic fiber, is being used as a new health food material in accordance with the progress in solubilization techniques for elastin. Objective: To evaluate the usefulness of elastin as a material for functional foods, we prepared highly pure, water-soluble elastin from pig aorta and evaluated its angiotensin-converting enzyme (ACE)-inhibitory activity. Method: Pure, water-soluble elastin was prepared from pig aorta using a hydrolyzing method employing a hot alkali reagent. Efficient enzymatic degradation of the elastin was achieved by using elastase that is specific for elastin. The ACE-inhibitory activities of elastin and of peptides obtained via enzymatic degradation were investigated. Three novel ACE-inhibiting peptides were purified from the degradation, and we investigated their ACE-inhibitory activities. Results: Highly pure, water-soluble elastin was prepared from pig aorta; this elastin preparation showed weak inhibitory activity (8.4% inhibition) against ACE. Surprisingly, 6-fold greater enzyme-inhibitory activity was observed for elastin peptides obtained from elastase-mediated degradation of the soluble elastin (48.0% inhibition). Among the enzymatically degraded elastin peptides, three were purified and their primary structures were newly characterized as Val-Tyr-Pro-Gly, Val-Gly-Val-Ala-Pro-Gly, and Gly-Tyr-Pro-Ile. All three peptides showed apparent ACE-inhibitory activity, and Val-Tyr-Pro-Gly exhibited the highest inhibitory capacity among them (60.6% inhibition). Conclusion: These results suggest that water-soluble elastin may serve as a functional food to exert a blood pressure-lowering effect in the body.

DOI： 10.2174/1573408013666170912113121

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85045381253&origin=inward

Stepwise Mechanism of Temperature-Dependent Coacervation of the Elastin-like Peptide Analogue Dimer, (C(WPGVG)<inf>3</inf>)<inf>2</inf> 査読有り

Tatsubo D., Suyama K., Miyazaki M., Maeda I., Nose T.

Biochemistry 57 ( 10 ) 1582 - 1590 2018年03月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are distinct, repetitive, hydrophobic sequences, such as (VPGVG)n, that exhibit coacervation, the property of reversible, temperature-dependent self-association and dissociation. ELPs can be found in elastin and have been developed as new scaffold biomaterials. However, the detailed relationship between their amino acid sequences and coacervation properties remains obscure because of the structural flexibility of ELPs. In this study, we synthesized a novel, dimeric ELP analogue (H-C(WPGVG)3-NH2)2, henceforth abbreviated (CW3)2, and analyzed its self-assembly properties and structural factors as indicators of coacervation. Turbidity measurements showed that (CW3)2 demonstrated coacervation at a concentration much lower than that of its monomeric form and another ELP. In addition, the coacervate held water-soluble dye molecules. Thus, potent and distinct coacervation was obtained with a remarkably short sequence of (CW3)2. Furthermore, fluorescence microscopy, dynamic light scattering, and optical microscopy revealed that the coacervation of (CW3)2 was a stepwise process. The structural factors of (CW3)2 were analyzed by molecular dynamics simulations and circular dichroism spectroscopy. These measurements indicated that helical structures primarily consisting of proline and glycine became more disordered at high temperatures with concurrent, significant exposure of their hydrophobic surfaces. This extreme change in the hydrophobic surface contributes to the potent coacervation observed for (CW3)2. These results provide important insights into more efficient applications of ELPs and their analogues, as well as the coacervation mechanisms of ELP and elastin.

DOI： 10.1021/acs.biochem.7b01144

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85043693562&origin=inward

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