Toke Orsolya, Tugyi Regina, Uray Katalin, Hudecz Ferenc
Institute of Structural Chemistry, Chemical Research Center, Hungarian Academy of Sciences, 59-67 Pusztaszeri út, Budapest H-1025, Hungary.
Biochem Biophys Res Commun. 2007 Jul 6;358(3):739-42. doi: 10.1016/j.bbrc.2007.04.200. Epub 2007 May 8.
High-molecular-weight mucin 2 (MUC2) glycoproteins show an aberrant glycosylation pattern when expressed in human colon carcinoma: the oligosaccharide chains are shorter and some are missing. In our ongoing effort of MUC2 vaccine development, we have solved the NMR structure of the all L-amino acid and various D-amino acid-substituted derivatives of the peptide TPTPTGTQTPT, previously identified as an epitope within the tandem repeat unit of the MUC2 glycoprotein. In the all L-amino acid containing peptide and in peptide tpTPTGTQtpt (where lowercase letters mark the position of D-amino acids) we identified a type I beta-turn spanning through residues (3)TPTG(6) and (5)TGTQ(8), respectively. Our structural findings are in good agreement with the antibody recognition properties of the investigated peptides and demonstrate that peptides with good stability against enzymatic degradation can be designed with good antibody binding characteristics.
高分子量粘蛋白2（MUC2）糖蛋白在人结肠癌中表达时呈现异常糖基化模式：寡糖链更短且有些缺失。在我们正在进行的MUC2疫苗开发工作中，我们解析了肽段TPTPTGTQTPT的全L-氨基酸以及各种D-氨基酸取代衍生物的核磁共振结构，该肽段先前被鉴定为MUC2糖蛋白串联重复单元内的一个表位。在含全L-氨基酸的肽段以及肽段tpTPTGTQtpt（小写字母标记D-氨基酸的位置）中，我们分别鉴定出一个跨越残基(3)TPTG(6)和(5)TGTQ(8)的I型β-转角。我们的结构研究结果与所研究肽段的抗体识别特性高度一致，并表明可以设计出对酶降解具有良好稳定性且具有良好抗体结合特性的肽段。
