Analysis of protein-carbohydrate interaction at the lower size limit of   the protein part (15-mer peptide) by NMR spectroscopy, electrospray   ionization mass spectrometry, and molecular modeling

doi:10.1021/bi025891x

CORC > 北京大学 > 生命科学学院

	Analysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling
	Siebert, HC ; Lu, SY ; Frank, M ; Kramer, J ; Wechselberger, R ; Joosten, J ; Andre, S ; Rittenhouse-Olson, K ; Roy, R ; von der Lieth, CW ; Kaptein, R ; Vliegenthart, JFG ; Heck, AJR ; Gabius, HJ
刊名	biochemistry us
	2002
关键词	DYNAMIC NUCLEAR-POLARIZATION ANTIBODY-BINDING PROPERTIES CELL-ADHESION MOLECULES RANA-CATESBEIANA EGGS T-ANTIGEN HEVEIN DOMAINS PEANUT LECTIN FORCE-FIELD 3-DIMENSIONAL STRUCTURE CONFORMER SELECTION
DOI	10.1021/bi025891x
英文摘要	Structural analysis of minimally sized lectins will offer insights into fundamentals of intermolecular recognition and potential for biomedical applications. We thus moved significantly beyond the natural limit of lectin size to determine the structure of synthetic mini-lectins in solution, their carbohydrate selectivity and the impact of ligand binding on their conformational behavior. Using three disaccharide (Thomsen-Friedenreich antigen; Galbeta1,3GalNAcalpha1,R)-binding pentadecapeptides without internal disulfide bridges as role models, we successfully tested a combined strategy with different techniques of NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling. In solution, the peptides invariably displayed flexibility with rather limited restrictions, shown by NMR experiments including nearly complete resonance assignments and molecular dynamics simulations. The occurrence of aromatic/nonpolar amino acids in the sequence did not lead to formation of a hydrophobic core known from microbial chitinase modules. Selectivity of disaccharide binding was independently observed by mass spectrometry and NMR analysis. Specific ligand interaction yielded characteristic NMR signal alterations but failed to reduce conformational flexibility significantly. We have thereby proven effectiveness of our approach to analyze even low-affinity interactions (not restricted to carbohydrates as ligands). It will be useful to evaluate the impact of rational manipulation of lead peptide sequences.; Biochemistry & Molecular Biology; SCI(E); 26; ARTICLE; 30; 9707-9717; 41
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/208855]
专题	生命科学学院
推荐引用方式 GB/T 7714	Siebert, HC,Lu, SY,Frank, M,et al. Analysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling[J]. biochemistry us,2002.
APA	Siebert, HC.,Lu, SY.,Frank, M.,Kramer, J.,Wechselberger, R.,...&Gabius, HJ.(2002).Analysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling.biochemistry us.
MLA	Siebert, HC,et al."Analysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling".biochemistry us (2002).