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Analysis of the immunogenicity and the ligand of Catesbeianalectin

Published: 2016-12-07

Keyword: Catesbeianalectin,peptide

Article from ourcustomer: Zhao Rui li. Chin J Biologicals. 2016

Keywords:Catesbeianalectin, peptide

Objective:Lectin can specifically bind to the glycoproteins or sugar chains on the surface of the cell membrane, and potentially can be used as a drug carrier. However, most of the lectins have immunogenicity, which limit their application. In this study, the immunogenicity of Catesbeianalectin, a novel bullfrog lectin, was analyzed, and the specific saccharide ligand of Catesbeianalectin was screened in vitro.

Results:The secondary structure of Catesbeianalectin was polyproline type 2 (PPII). The mean serum antibody titer was 1: 200, 1: 1600, and 1:25 against OVA, WGA, and Catesbeianalectin in mice, respectively. Catesbeianalectin mainly interacted with galactosyl and polysaccharide containing galactose when it passed through the 30 kinds of monose fixed on the biochip.

Conclusion :Catesbeianalectin showed low immunogenicity. It was an S-lection, which binds to the polysaccharide containg galactosyl in vitro. It has laid a foundation for using Catesbeianalectin as a drug carrier.

 


Catesbeianlectin was synthesized according to the standard solid phase peptide synthesisby ZheJiang Ontores Biotechnologies Co. Ltd. (Hangzhou, China). It was desalted and purified by the HPLC (waters 600 controller) reversed phase C18 column chromatography. The relative molecular mass was determined by the fast atom bombardment mass spectrometry (AB3200).