Mapping the Binding Sites of MMPs on Types II and III Collagens Using Triple-Helical Peptide Toolkits.

Mapping the Binding Sites of MMPs on Types II and III Collagens Using Triple-Helical Peptide Toolkits.
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使用三螺旋肽工具包绘制 II 型和 III 型胶原上 MMP 的结合位点。

DOI:
10.1007/978-1-0716-3589-6_7
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发表时间:
2024
期刊:
Methods in molecular biology (Clifton, N.J.)
影响因子:
--
通讯作者:
Manka SW
Manka SW
中科院分区:
--
文献类型:
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作者:
Manka SW

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三螺旋胶原蛋白样肽库(胶原蛋白工具包)已帮助定义许多胶原蛋白结合蛋白的胶原蛋白II和III结合特异性。在这里,我描述了一个简单的固相结合试验,利用生物素-链霉亲和素系统筛选胶原工具包的结合两个不同的基质金属蛋白酶(MMP)参与癌症:胶原蛋白溶解MMP 1(胶原酶1)和非胶原蛋白溶解MMP 3(基质分解素1)。筛选揭示了这些MMPs在胶原蛋白II和III上的明显不同的结合足迹,与其不同的生物活性一致。其他潜在的胶原蛋白结合蛋白酶的类似筛选可能揭示其固有的组织保留能力和其促或抗转移的潜力。
Libraries of triple-helical collagen-like peptides (Collagen Toolkits) have helped to define collagens II and III binding specificities of numerous collagen-binding proteins. Here I describe a simple solid-phase binding assay utilizing a biotin–streptavidin system to screen the Collagen Toolkits for binding of two distinct matrix metalloproteinases (MMPs) implicated in cancer: the collagenolytic MMP1 (collagenase 1) and the non-collagenolytic MMP3 (stromelysin 1). The screening revealed markedly disparate binding footprints of these MMPs on collagens II and III, in line with their distinct biological activities. Analogous screening of other potentially collagen-binding proteases may shed light on their inherent tissue retention capabilities and their pro- or anti-metastatic potential.