Robust cross-links in molluscan adhesive gels: testing for contributions from hydrophobic and electrostatic interactions.

Robust cross-links in molluscan adhesive gels: testing for contributions from hydrophobic and electrostatic interactions.
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DOI:
10.1016/j.cbpb.2008.10.004
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发表时间:
2009-02
影响因子:
2.2
通讯作者:
Blasiak, R.
Blasiak, R.
中科院分区:
生物学3区
文献类型:
--
作者:
Smith, A. M.;Robinson, T. M.;Salt, M. D.;Hamilton, K. S.;Silvia, B. E.;Blasiak, R.

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研究了为软体动物粘合剂凝胶提供内聚强度的交联相互作用。基于金属的相互作用已被证明在蛞蝓Arion subfuscus(Draparnaud)的胶水中发挥重要作用,但其他类型的相互作用也可能有助于胶水的强度,它们的作用尚未被研究。这项研究表明,通常破坏疏水或静电相互作用的处理对段塞胶几乎没有影响。高盐浓度和非离子型去污剂不影响蛋白质在胶中的溶解度或胶蛋白质溶解凝胶的能力。相比之下,金属螯合作用明显破坏凝胶。凝胶过滤色谱实验鉴定了一种40 kDa的蛋白质,该蛋白质是胶中交联的中心组分。这种40 kDa蛋白质形成坚固的大分子聚集体,即使在高浓度的盐、非离子去污剂、尿素或金属螯合剂存在下也是稳定的。然而,胶分泌过程中的金属螯合作用可能会阻止其中一些交联。在水性环境中这种稳健的非特异性相互作用对于水凝胶来说是非常不寻常的,并且反映了一种有趣的交联机制。
The cross-linking interactions that provide cohesive strength to molluscan adhesive gels were investigated. Metal-based interactions have been shown to play an important role in the glue of the slug Arion subfuscus (Draparnaud), but other types of interactions may also contribute to the glue's strength and their role has not been investigated. This study shows that treatments that normally disrupt hydrophobic or electrostatic interactions have little to no effect on the slug glue. High salt concentrations and non-ionic detergent do not affect the solubility of the proteins in the glue or the ability of the glue proteins to stiffen gels. In contrast, metal chelation markedly disrupts the gel. Experiments with gel filtration chromatography identify a 40 kDa protein that is a central component of the cross-links in the glue. This 40 kDa protein forms robust macromolecular aggregations that are stable even in the presence of high concentrations of salt, non-ionic detergent, urea or metal chelators. Metal chelation during glue secretion, however, may block some of these cross-links. Such robust, non-specific interactions in an aqueous environment are highly unusual for hydrogels and reflect an intriguing cross-linking mechanism.
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