Bayard Fabrice, Raveneau Amélie, Letourneau Aurélie, Joucla Gilles, Barbot Caroline, Garbay Bertrand, Cabanne Charlotte
EA 4135, Ecole Supérieure de Technologie des Biomolécules de Bordeaux, Université Victor Segalen Bordeaux2, 146 rue Leo Saignat, 33076 Bordeaux Cedex, France.
Anal Biochem. 2009 Jan 15;384(2):350-2. doi: 10.1016/j.ab.2008.10.016. Epub 2008 Oct 19.
Antimicrobial peptides (AMPs) are cationic molecules that are good leads for new antiinfective drugs. To obtain sufficient amounts, recombinant AMPs are generally produced as fusion proteins in Escherichia coli. Fusion partners facilitate purification of recombinant proteins. Fusion proteins are then cleaved by specific proteases, and cationic peptides are purified by size exclusion chromatography or ion exchange chromatography, neither of which is easily applicable to small volumes of diluted peptide samples. We developed a small-scale system that is easily adaptable for high-throughput screening and uses carboxyl magnetic beads to purify a cationic peptide from its fusion partner.
抗菌肽（AMPs）是阳离子分子，是新型抗感染药物的良好先导物。为了获得足够的量，重组抗菌肽通常在大肠杆菌中作为融合蛋白产生。融合伙伴有助于重组蛋白的纯化。然后通过特定蛋白酶切割融合蛋白，阳离子肽通过尺寸排阻色谱法或离子交换色谱法纯化，这两种方法都不容易应用于少量稀释的肽样品。我们开发了一种小规模系统，该系统易于适应高通量筛选，并使用羧基磁珠从其融合伙伴中纯化阳离子肽。
