Hydrogel Scaffolds of Amphiphilic and Acidic β-Sheet Peptides
Hydrogel Scaffolds of Amphiphilic and Acidic β-Sheet Peptides
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DOI：
10.1002/adfm.200800117
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发表时间：
2008-10-09
影响因子：
19
通讯作者：
Silberstein, Tova
中科院分区：
文献类型：
--
作者：
Rapaport, Hanna;Grisaru, Haviv;Silberstein, Tova
具有Pro-Y-(Z-Y)(5)- pro, Y = Glu或Asp， Z = Phe或Leu序列的两亲性和酸性p -片形成肽（AA β Ps）可以在接近中性的pH值下组装成水凝胶结构，比其酸性氨基酸侧链的固有pKa高几个单位。自下而上的设计策略使肽的氨基酸组成和整体pH水解之间的合理支持关联。在-片结构中，酸性氨基酸侧链之间的氢键对AA - β - Ps水凝胶的稳定起着重要作用。带负电荷的肽也被发现在钙离子存在的情况下形成低浓度的凝胶。骨形成细胞可以在生理pH值下形成的AA β - Ps水凝胶的二维膜上培养，也可以在三维水凝胶基质中培养。这些富含酸的多肽水凝胶在矿化组织的工程应用中具有优势，为影响生物活性和无机矿化提供了可控的、多功能的钙化支架。
Amphiphilic and acidic P-sheet-forming peptides (AA beta Ps) having the sequence Pro-Y-(Z-Y)(5)-Pro, Y = Glu or Asp and Z = Phe or Leu may assemble into hydrogel structures at near neutral pH values, several units higher than the intrinsic pKa of their acidic amino acid side chains. The bottom-to-top design strategy enables the rationally supported association between the peptides' amino acids composition and bulk pH hydrogelation. Hydrogen bonds between the acidic amino acids side chains in the beta-sheet structure are found to contribute substantially to the stabilization of AA beta Ps hydrogels. The negatively charged peptides are also found to form gels at lower concentration in presence of calcium ions. Bone forming cells may be cultured on two-dimensional films of AA beta Ps hydrogels that form at physiological pH values as well as within three dimensional hydrogel matrices. These acidic-rich peptides hydrogels may become advantageous in applications related to engineering of mineralized tissues providing controllable, multifunctional calcified scaffolds to affect both the biological activity and the inorganic mineralization.