Regulation of in vitro calcium phosphate mineralization by combinatorially selected hydroxyapatite-binding peptides
Regulation of in vitro calcium phosphate mineralization by combinatorially selected hydroxyapatite-binding peptides
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DOI：
10.1021/bm701037x
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发表时间：
2008-03-01
影响因子：
6.2
通讯作者：
Sarikaya, Mehmet
中科院分区：
文献类型：
--
作者：
Gungormus, Mustafa;Fong, Hanson;Sarikaya, Mehmet
我们报道了从噬菌体肽库中筛选和鉴定与羟基磷灰石结合的七肽，并展示了两种具有不同结合亲和力和结构性质的多肽对磷酸钙矿物矿化的影响。分别使用一个强结合肽和一个弱结合肽HABP1和HABP2进行的体外矿化研究表明，前者在矿化动力学和颗粒形态上表现出强烈的结果。在电子显微镜下观察到，与在弱结合多肽存在下或在阴性对照中形成的那些相比，强结合多肽产生了明显更大的晶体。圆二色谱的分子结构研究表明，HABP1和HABP2的二级结构和构象稳定性不同。结果表明，序列、结构和分子稳定性对这些多肽的矿化活性有很大影响。这项研究的意义在于，组合选择的短序列多肽可能通过控制磷酸钙生物矿物质的形成而用于硬组织的修复或再生。
We report selection and characterization of hydroxyapatite-binding heptapeptides from a peptide-phage library and demonstrate the effects of two peptides, with different binding affinities and structural properties, on the mineralization of calcium phosphate mineral. In vitro mineralization studies carried out using one strong- and one weak-binding peptide, HABP1 and HABP2, respectively, revealed that the former exhibited a drastic outcome on mineralization kinetics and particle morphology. Strong-binding peptide yielded significantly larger crystals, as observed by electron microscopy, in comparison to those formed in the presence of a weak-binding peptide or in the negative control. Molecular structural studies carried out by circular dichoroism revealed that HABP1 and HABP2 differed in their secondary structure and conformational stability. The results indicate that sequence, structure, and molecular stability strongly influence the mineralization activity of these peptides. The implication of the research is that the combinatorially selected short-sequence peptides may be used in the restoration or regeneration of hard tissues through their control over of the formation of calcium phosphate biominerals.