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
N1 - Funding Information:
We thank Dr. Ayami Matsushima (Faculty of Science, Kyushu University) for equipment use and her help in CD spectra measurement. We also thank Drs. Tamotsu Kiyoshima, Kunio Ishikawa, Koichiro Hayashi, and Ryo Kishida (Faculty of Dental Science, Kyushu university) for equipment use in laser diffraction particle size measurement. This work was supported by JSPS KAKENHI grant numbers JP26550068 and JP17K20066. We also thank E&C HealthCare, Ltd. and ECC Co., Ltd. for financial support.
Publisher Copyright:
© 2018 American Chemical Society.
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.
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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 -