Mussel-inspirit polymerization: „The enzyme free route of an tyrosinase activated polymerization“

贻贝激发聚合：“酪氨酸酶激活聚合的无酶途径”

• 批准号: 234499734
• 负责人: Professor Dr. Hans Gerhard Börner
• 金额: --
• 依托单位: Institut für Chemie
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2013
• 资助国家: 德国
• 起止时间: 2012-12-31 至 2023-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/234499734?language=en
• 关键词: Mussel; inspirit; polymerization; enzyme; free

Research objective of the proposal is the introduction of a novel class of macromonomers, which provides the possibility to exhibit a polymerization after being enzymatically activated. As a result of the enzyme activated polymerization, segmented copolymers with multifunctional character will be obtained. The polymerization process is derived from the fundamental cross-linking principle occurring in mussel adhesion processes. Similar chemistry that leads during byssus formation of marine mussels to cross-links between mussel foot proteins should be employed to generate linear polymers with repetitive monomer sequences.During mussel adhesion, enzymatically controlled processes occur, which synchronize the activation and crosslinking of a set of mussel foot proteins. The process is highly complex and far from being fully understood, but the fundamental cross-linking principle can be abstracted and applied towards linear polymerization of designed oligopeptides (macromonomers) yielding segmented copolymers.The enzymatically activatable and polymerizable oligopeptides require to have one tyrosine residue and one lysine or cysteine residue. This will allow for the two-step polymerization process to occur: First the non-polymerizalble oligopeptide will be enzymatically activated by tyrosinase, generating a 3,4-dihydroxyphenylalanin derivative (L-Dopa derivative) from the tyrosine residue. Subsequently, polymerization can occur by polyaddition mechanism involving the michel addition of the nucleophilic side chain functionality of lysine or cysteine (amino or thiol) to the L-Dopa derivative leading to lysinyl-DOPA- or cycteinyl-DOPA coupling products, respectively.Within the project the minimum requirements for a tyrosinase activatable macromonomer and the maximum tolerance of the process towards deviation from biologically derived tyrosinase substrates will be investigated. A set of functional macromonomers will be synthesized, the tyrosinase activation-kinetics and the following polymerization mechanism will be investigated. The polymerization process will be adapted to a larger scale of up to 1-10 g macromonomers and the multifunctional polymers will be deeply characterized, before being tested as coatings for various material surfaces. Besides revealing insight into fundamental aspects of bioadhesion, interesting polymers will be accessed that might have potential as adhesives, (nano)particle stabilizers, or crystal growth modifiers.

该提案的研究目标是引入一类新的大分子单体，其提供了在酶促活化后显示聚合的可能性。酶活化聚合的结果是得到具有多功能特性的嵌段共聚物。聚合过程源自贻贝粘附过程中发生的基本交联原理。在贻贝足丝形成过程中，贻贝足蛋白之间发生交联的类似化学反应应该被用来产生具有重复单体序列的线性聚合物。在贻贝粘附过程中，发生酶促控制的过程，这同步了一组贻贝足蛋白的活化和交联。这个过程非常复杂，还远未完全理解，但基本的交联原理可以抽象并应用于设计的寡肽（大分子单体）的线性聚合，产生嵌段共聚物。这将允许两步聚合过程发生：首先，不可聚合的寡肽将被酪氨酸酶酶促活化，从酪氨酸残基产生3，4-二羟基苯丙氨酸衍生物（L-多巴衍生物）。随后，聚合可通过涉及赖氨酸或半胱氨酸的亲核侧链官能团的Michel加成的加聚机理发生- 将（氨基或巯基）与L-多巴衍生物结合，产生赖氨酸基-多巴-或半胱氨酸基-多巴偶联产物，在该项目中，对酪氨酸酶可活化大分子单体的最低要求和该方法对生物衍生酪氨酸酶底物偏差的最大耐受性将追究本研究将合成一系列功能性大分子单体，并探讨酪氨酸酶活化动力学及后续聚合反应机理。聚合过程将适用于高达1-10 g大分子单体的更大规模，并且在作为各种材料表面的涂层进行测试之前，将对多官能聚合物进行深入表征。除了揭示生物粘附的基本方面，有趣的聚合物将被访问，可能有潜力作为粘合剂，（纳米）颗粒稳定剂，或晶体生长改性剂。