Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG) n Using Nitrilotriacetic Acid as a Building Block

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

doi:10.1021/acsomega.0c06140

Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG) _n Using Nitrilotriacetic Acid as a Building Block

ACS Omega. 2021 Feb 18;6(8):5705-5716. doi: 10.1021/acsomega.0c06140. eCollection 2021 Mar 2.

Authors

Keitaro Suyama¹, Mika Mawatari², Daiki Tatsubo², Iori Maeda³, Takeru Nose^{1

2}

Affiliations

¹ Laboratory of Biomolecular Chemistry, Faculty of Arts and Science, Kyushu University, Fukuoka 819-0395, Japan.
² Department of Chemistry, Faculty and Graduate School of Science, Fukuoka 819-0395, Japan.
³ Department of Physics and Information Technology, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Japan.

Abstract

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.