Design of Phenylalanine-Containing Elastin-Derived Peptides Exhibiting Highly Potent Self-Assembling Capability
Design of Phenylalanine-Containing Elastin-Derived Peptides Exhibiting Highly Potent Self-Assembling Capability
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DOI：
10.2174/092986652210150821170703
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发表时间：
2015-01-01
影响因子：
1.6
通讯作者：
Nose, Takeru
中科院分区：
文献类型：
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作者：
Maeda, Iori;Taniguchi, Suguru;Nose, Takeru
在本研究中，我们开发了一系列含Phe的弹性蛋白衍生肽类似物（Phe-Pro-Gly-Val-Gly）（n）（n = 1-5），并分析了它们的可逆凝聚性质。与天然弹性蛋白衍生的重复肽序列（（Val-Pro-Gly-Val-Gly）（10））相比，含Phe的5-mer重复肽序列之一（（Phe-Pro-Gly-Val-Gly）（5））明显表现出更强的凝聚性质。（Phe-Pro-Gly-Val-Gly）（5）与多肽（Val-Pro-Gly-Val-Gly）（n）（n > 40）的凝聚力基本相同。尽管弹性蛋白衍生肽的凝聚通常需要大分子量（> 10，000 Da），但（Phe-Pro-Gly-Val-Gly）（5）尽管分子量低（MW = 2，305 Da），但仍表现出可逆凝聚特性。高效液相色谱（HPLC）和圆二色性（CD）分析表明（Phe-Pro-Gly-Val-Gly）（5）具有高疏水性和具有II型β转角的有序结构，这有助于肽的强凝聚能力。此外，（Phe-Pro-Gly-Val-Gly）（5）在体温（37 ℃）下表现出有效的粒度分布（60-70 nm），并且在低温下表现出与单体肽相似的分散的小粒度。这些特性，沿着其小尺寸和简单设计，使得肽适合用于生物材料，包括药物递送载体。
In this study, we developed a series of Phe-containing elastin-derived peptide-analogs, (Phe-Pro-Gly-Val-Gly)(n) (n = 1-5) and analyzed their reversible coacervation properties. Compared to the native elastin-derived repeating peptide sequence ((Val-Pro-Gly-Val-Gly)(10)), one of the Phe-containing 5-mer repeating peptide sequences ((Phe-Pro-Gly-Val-Gly)(5)) clearly exhibited stronger coacervation properties. The coacervation of (Phe-Pro-Gly-Val-Gly)(5) is nearly the same as that of polypeptides (Val-Pro-Gly-Val-Gly)(n) (n > 40). Although large molecular weights (>10,000 Da) are generally required for the coacervation of elastin-derived peptides, (Phe-Pro-Gly-Val-Gly)(5) exhibited reversible coacervation properties despite its low molecular weight (MW = 2,305 Da). High performance liquid chromatography (HPLC) and circular dichroism (CD) analysis revealed that (Phe-Pro-Gly-Val-Gly)(5) has high hydrophobicity and an ordered structure with a type II beta-turn, which contributes to the strong coacervation ability of the peptide. In addition, (Phe-Pro-Gly-Val-Gly)(5) exhibited an effective particle size distribution (60-70 nm) at body temperature (37 degrees C) and a dispersed small particle size similar to that of the monomer peptides at low temperatures. These properties, along with its small size and simple design, render the peptide suitable for use in biomaterials, including drug-delivery carriers.