Abstract
Elastin-like peptides (ELP) 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 thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its 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.
| Original language | English |
|---|---|
| Pages (from-to) | 3201-3211 |
| Number of pages | 11 |
| Journal | Biomacromolecules |
| Volume | 19 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Jun 22 2018 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Bioengineering
- Biomaterials
- Polymers and Plastics
- Materials Chemistry
Cite this
Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization : strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids. / Suyama, Keitaro; Tatsubo, Daiki; Iwasaki, Wataru; Miyazaki, Masaya; Kiyota, Yuhei; Takahashi, Ichiro; Maeda, Iori; Nose, Takeru.
In: Biomacromolecules, Vol. 19, No. 8, 22.06.2018, p. 3201-3211.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization
T2 - strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids
AU - Suyama, Keitaro
AU - Tatsubo, Daiki
AU - Iwasaki, Wataru
AU - Miyazaki, Masaya
AU - Kiyota, Yuhei
AU - Takahashi, Ichiro
AU - Maeda, Iori
AU - Nose, Takeru
PY - 2018/6/22
Y1 - 2018/6/22
N2 - Elastin-like peptides (ELP) 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 thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its 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.
AB - Elastin-like peptides (ELP) 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 thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its 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.
UR - http://www.scopus.com/inward/record.url?scp=85049214569&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85049214569&partnerID=8YFLogxK
U2 - 10.1021/acs.biomac.8b00353
DO - 10.1021/acs.biomac.8b00353
M3 - Article
C2 - 29932654
AN - SCOPUS:85049214569
VL - 19
SP - 3201
EP - 3211
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
IS - 8
ER -