title: Development of short and highly potent self-assembling elastin-derived pentapeptide repeats containing aromatic amino acid residues.
abstract: Tropoelastin is the primary component of elastin, which forms the elastic fibers that make up connective tissues. The hydrophobic domains of tropoelastin are thought to mediate the self-assembly of elastin into fibers, and the temperature-mediated self-assembly (coacervation) of one such repetitive peptide sequence (VPGVG) has been utilized in various bio-applications. To elucidate a mechanism for coacervation activity enhancement and to develop more potent coacervatable elastin-derived peptides, we synthesized two series of peptide analogs containing an aromatic amino acid, Trp or Tyr, in addition to Phe-containing analogs and tested their functional characteristics. Thus, position 1 of the hydrophobic pentapeptide repeat of elastin (X(1)P(2)G(3)V(4)G(5)) was substituted by Trp or Tyr. Eventually, we acquired a novel, short Trp-containing elastin-derived peptide analog (WPGVG)3 with potent coacervation ability. From the results obtained during this process, we determined the importance of aromaticity and hydrophobicity for the coacervation potency of elastin-derived peptide analogs. Generally, however, the production of long-chain synthetic polypeptides in quantities sufficient for commercial use remain cost-prohibitive. Therefore, the identification of (WPGVG)3, which is a 15-mer short peptide consisting simply of five natural amino acids and shows temperature-dependent self-assembly activity, might serve as a foundation for the development of various kinds of biomaterials.
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.
authors.forename: Suguru
authors.initials: S
authors.lastname: Taniguchi
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.
authors.forename: Noriko
authors.initials: N
authors.lastname: Watanabe
authors.affiliation: Faculty of Arts and Science, Kyushu University, Fukuoka, 819-0395, Japan.
authors.forename: Takeru
authors.initials: T
authors.lastname: Nose
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.
authors.forename: Iori
authors.initials: I
authors.lastname: Maeda
mesh_terms: D000595:Amino Acid Sequence; D024322:Amino Acids, Aromatic / Q000737:chemistry*; D004549:Elastin / Q000737:chemistry*; D005427:Flocculation; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D060327:Solid-Phase Synthesis Techniques / Q000379:methods*; D013329:Structure-Activity Relationship; D013696:Temperature; D014333:Tropoelastin / Q000737:chemistry*
chemical_list: D024322:Amino Acids, Aromatic; D010455:Peptides; D014333:Tropoelastin; D004549:Elastin
keywords: aromatic amino acids; circular dichroism; coacervation; elastin-derived peptide