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青岛双元泰和药业有限公司

青岛市城阳区双元路218号

电话: 0532-55676230
传真: 0532-55676180

疏水肽


双元泰和疏水性多肽合成基于专有的技术平台,为您提供研究级的定制多肽和疏水肽。

什么是疏水肽技术


双元泰和疏水肽技术包括:

  1. 混合合成平台: 固相多肽合成(SPPS)/ 液相多肽合成 (LPPS), 连接技术和裂碎技术
  2. 联合纯化平台:
    • 凝胶渗透色谱(GPC)
    • 离子交换色谱(IEC)
    • 反相高效液相色谱(RP-HPLC)
    疏水肽技术改善合成效率,下图描述了合成过程: HydroFobic Peptide technology

    为什么开发疏水肽技术?

    单个蛋白质的3D结构以及生物活性主要由其组分氨基酸的一级序列决定。肽链形成有序结构的固有倾向是在肽组装期间遇到的合成效率的高度序列特异性变异性的主要原因。由于肽是细长的,它可以与其他肽链或聚合物载体形成二级结构或聚集体,这可导致较低的反应速率。该效应可以仅从微妙的减速到脱保护和酰化反应的完全失效。在这种极端情况下,多肽变得不溶,不再可用于反应。给定序列的空间结构通常难以预测,尽管含有连续疏水性氨基酸的片段如Ala,Val,Ile以及含有可以形成链内氢键氨基酸(如Gln和Thr)的多肽常常难以制备,这是使多肽合成有趣和具有挑战性的因素之一。因此,一般来说,最好从开始的合成策略中采用减轻结构形成的方案,而不是尝试第二次猜测哪些肽可能是有问题的而浪费时间和资源重复失败的合成。为此,双元泰和开发了疏水肽技术,解决了大部分问题。

    多肽为什么合成困难?

    描述 解释
    Multiple Aspartic Acids (D) Multiple Aspartic Acids (D) in a sequence frequently result in the formation of aspartimide adducts, resulting in a product of lower purity.
    Adjacent Serines (S) Adjacent Serines (-AA-S-) in a sequence frequently result in product that is low in purity and/or contain many deletions
    Poly(GGGG) Multiple consecutive Glycines (G) (4 or more) tend to undergo hydrogen bonding (gel formation) in the peptide backbone. The hydrogen bonding may cause difficulty in dissolving and purifying the peptide
    Difficult amino acids: C, M, W Especially in summer, it's easily to oxidation if peptide containing C or M or W
    >75% hydrophobic residues, and contains 25% charged residues May be insoluble or only partially soluble in aqueous solutions
    >50% hydrophobic residues, and contains 25% negative charged residues May be insoluble or only partially soluble in aqueous solutions
    >50% to 75% hydrophobic residues and without charged residues May be insoluble or only partially soluble in aqueous solutions
    Very hydrophobic peptides containing >75% hydrophobic residues Generally not dissolve in aqueous solutions
    Secondary Structure: The peptide containing streches of contiguous hydrophobic amino acids: Val, Ile, Ala as well as those containing amino acids wich can form intra-chain or inter-chain hydrogen bonds, such as Gln or Thr. During synthesis, ?-sheet formation causes incomplete solvation of the growing peptide and results in a high degree of deletion sequences in the final product.