WALTZ-DB: a benchmark database of amyloidogenic hexapeptides

被引:62
作者
Beerten, Jacinte [1 ,2 ]
Van Durme, Joost [1 ,2 ]
Gallardo, Rodrigo [1 ,2 ]
Capriotti, Emidio [1 ,2 ,3 ]
Serpell, Louise [4 ]
Rousseau, Frederic [1 ,2 ]
Schymkowitz, Joost [1 ,2 ]
机构
[1] VIB Switch Lab, Leuven, Belgium
[2] Katholieke Univ Leuven, Dept Cellular & Mol Med, Leuven, Belgium
[3] Univ Alabama Birmingham, Dept Pathol, Div Informat, Birmingham, AL 35249 USA
[4] Univ Sussex, Sch Life Sci, Falmer BN1 9QG, E Sussex, England
关键词
AGGREGATION; PROTEINS; PREDICTION; PEPTIDES; SERVER;
D O I
10.1093/bioinformatics/btv027
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Accurate prediction of amyloid-forming amino acid sequences remains an important challenge. We here present an online database that provides open access to the largest set of experimentally characterized amyloid forming hexapeptides. To this end, we expanded our previous set of 280 hexapeptides used to develop the Waltz algorithm with 89 peptides from literature review and by systematic experimental characterisation of the aggregation of 720 hexapeptides by transmission electron microscopy, dye binding and Fourier transform infrared spectroscopy. This brings the total number of experimentally characterized hexapeptides in the WALTZ-DB database to 1089, of which 244 are annotated as positive for amyloid formation.
引用
收藏
页码:1698 / 1700
页数:3
相关论文
共 14 条
[1]   Rationalization of the effects of mutations on peptide and protein aggregation rates [J].
Chiti, F ;
Stefani, M ;
Taddei, N ;
Ramponi, G ;
Dobson, CM .
NATURE, 2003, 424 (6950) :805-808
[2]   CONFORMATIONAL PARAMETERS FOR AMINO-ACIDS IN HELICAL, BETA-SHEET, AND RANDOM COIL REGIONS CALCULATED FROM PROTEINS [J].
CHOU, PY ;
FASMAN, GD .
BIOCHEMISTRY, 1974, 13 (02) :211-222
[3]  
De Baets G, 2014, ESSAYS BIOCHEM, V56, P41, DOI [10.1042/bse0560041, 10.1042/BSE0560041]
[4]  
Eisenberg D, 2005, FEBS J, V272, P78
[5]  
Eisenberg D, 2009, FASEB J, V23
[6]   The Amyloid State of Proteins in Human Diseases [J].
Eisenberg, David ;
Jucker, Mathias .
CELL, 2012, 148 (06) :1188-1203
[7]   Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins [J].
Fernandez-Escamilla, AM ;
Rousseau, F ;
Schymkowitz, J ;
Serrano, L .
NATURE BIOTECHNOLOGY, 2004, 22 (10) :1302-1306
[8]   Functional amyloid formation within mammalian tissue [J].
Fowler, DM ;
Koulov, AV ;
Alory-Jost, C ;
Marks, MS ;
Balch, WE ;
Kelly, JW .
PLOS BIOLOGY, 2006, 4 (01) :100-107
[9]   Human pancreatitis-associated protein forms fibrillar aggregates with a native-like conformation [J].
Ho, Meng-Ru ;
Lou, Yuan-Chao ;
Lin, Wen-Chang ;
Lyu, Ping-Chiang ;
Huang, Wei-Ning ;
Chen, Chinpan .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (44) :33566-33576
[10]  
Maurer-Stroh S, 2010, NAT METHODS, V7, P237, DOI [10.1038/NMETH.1432, 10.1038/nmeth.1432]