为了促使多肽亲和配基在实际分离研究中得到广泛应用，利用Fmoc固相合成法对从噬菌体展示肽库中筛选得到的与胰岛素具有高特异性亲和的七肽片段（HWWWPAS）进行了合成。在合成中发现，肽段序列中脯氨酸的存在会严重影响合成结果。云除脯氨酸后，目标产物的收率从0%提高到11.6%；同时，七肽序列中丙氨酸的存在也会影响合成效果。若将丙氨酸除去，合成收率会明显提高（达到76%），特别是将丙氨酸更换为谷氨酸产物的收率和线度可达到70%以上。利用固定化六肽片段（HWWWES）进行亲和吸附实验的结果表明，改造后的六肽配基与原先的七肽配基具有相似的亲和吸附效果。

From the renaturation kinetics of denatured/reduced lysozyme assisted by the molecular chaperone GroEL, a simplified kinetic model was established based on the competition between protein folding and aggregation. In the presence of GroEL and ATP, the aggregate formation was a second order reaction. With 2mM ATP, a renaturation yield of 90% at a high renaturation rate was obtained when the molar ratio of GroEL to lysozyme was 1: 1.

Protein renaturation is of importance in the recovery of inclusion-body protein produced by recombinant microbial cells. It has been recognized that the artificial chaperone system, Cetyltrimethylammonium bromide and β-cyclodextrin, are effective in enhancing protein renaturation. Using chicken egg white lysozyme as a model protein, this work studied protein renaturation by size exclusion chromatography (SEC) incorporating with the artificial chaperone system. At first, a cooperative effect of the artificial chaperones and guanidinium chloride (GdmCl) on the protein renaturation was confirmed, and it was concluded that the artificial chaperone system promoted the renaturation of lysozyme (1.05mg/ml) in the presence of 1mol/liter GdmCl. Using the SEC (29.5×2.6cm I.D., packed with Sephacryl S-100h gel) incorporating with the artificial chaperones, higher renaturation yield was obtained at high flow rate (0.8-2.2ml/min). In contrast, using the SEC without the artificial chaperones, very low flow rate (i.e.<0.4ml/min) should be used to receive a comparable renaturation yield. Thus, use of the SEC incorporating with the artificial chaperone system would greatly benefit in reaching a high refolding productivity.