FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

被引:20
作者
Stawoska, Iwona [1 ]
Weselucha-Birczynska, Aleksandra [2 ]
Skoczowski, Andrzej [1 ,3 ]
Dziurka, Michal [3 ]
Waga, Jacek [4 ]
机构
[1] Pedag Univ Krakow, Inst Biol, Podchorazych 2, PL-30084 Krakow, Poland
[2] Jagiellonian Univ, Fac Chem, Gronostajowa 2, PL-30387 Krakow, Poland
[3] Polish Acad Sci, Franciszek Gorski Inst Plant Physiol, Niezapominajek 21, PL-30239 Krakow, Poland
[4] Univ Agr, Dept Physiol Plant Breeding & Seed Sci, Podluzna 3, PL-30239 Krakow, Poland
来源
MOLECULES | 2021年 / 26卷 / 17期
关键词
gluten proteins; gliadins; amide I; secondary structure; Raman spectroscopy; GLUTEN PROTEINS; DISULFIDE BONDS; IGE-BINDING; RESONANCE RAMAN; IDENTIFICATION; EPITOPES; SPECTRA; ALLERGY; FOOD; EPR;
D O I
10.3390/molecules26175388
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Raman spectroscopy is a useful method in biological, biomedical, food, and agricultural studies, allowing the simultaneous examination of various chemical compounds and evaluation of molecular changes occurring in tested objects. The purpose of our research was to explain how the elimination of omega-fractions from the wheat gliadin complex influences the secondary structures of the remaining alpha beta gamma-gliadins. To this aim, we analyzed the endosperm of wheat kernels as well as gliadin proteins extracted from two winter wheat genotypes: wasko.gl+ (control genotype containing the full set of gliadins) and wasko.gl- (modified genotype lacking all omega-gliadins). Based on the decomposition of the amide I band, we observed a moderate increase in beta-forms (sheets and turns) at the expense of alpha-helical and random coil structures for gliadins isolated from the flour of the wasko.gl- line. Since omega-gliadins contain no cysteine residues, they do not participate in the formation of the disulfide bridges that stabilize the protein structure. However, they can interact with other proteins via weak, low-energetic hydrogen bonds. We conclude that the elimination of omega-fractions from the gliadin complex causes minor modifications in secondary structures of the remaining gliadin proteins. In our opinion, these small, structural changes of proteins may lead to alterations in gliadin allergenicity.
引用
收藏
页数:18
相关论文
共 81 条
[1]   Determination of amylose content in starch using Raman spectroscopy and multivariate calibration analysis [J].
Almeida, Mariana R. ;
Alves, Rafael S. ;
Nascimbem, Laura B. L. R. ;
Stephani, Rodrigo ;
Poppi, Ronei J. ;
de Oliveira, Luiz Fernando C. .
ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 2010, 397 (07) :2693-2701
[2]  
[Anonymous], 1982, Raman Spectroscopy in Biology: Principles and Applications
[3]   In situ simultaneous analysis of polyacetylenes, carotenoids and polysaccharides in carrot roots [J].
Baranska, M ;
Schulz, H ;
Baranski, R ;
Nothnagel, T ;
Christensen, LP .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2005, 53 (17) :6565-6571
[4]   Targeting of prolamins by RNAi in bread wheat: effectiveness of seven silencing-fragment combinations for obtaining lines devoid of coeliac disease epitopes from highly immunogenic gliadins [J].
Barro, Francisco ;
Iehisa, Julio C. M. ;
Gimenez, Maria J. ;
Garcia-Molina, Maria D. ;
Ozuna, Carmen V. ;
Comino, Isabel ;
Sousa, Carolina ;
Gil-Humanes, Javier .
PLANT BIOTECHNOLOGY JOURNAL, 2016, 14 (03) :986-996
[5]   Identification of IgE-binding epitopes on gliadins for patients with food allergy to wheat [J].
Battais, F ;
Mothes, T ;
Moneret-Vautrin, DA ;
Pineau, F ;
Kanny, G ;
Popineau, Y ;
Bodinier, M ;
Denery-Papini, S .
ALLERGY, 2005, 60 (06) :815-821
[6]  
Becker D., 2006, Getreidetechnologie, V60, P153
[7]  
Bietz J.A., 2002, HPLC BIOL MACROMOLEC, P547
[8]   WHEAT CULTIVAR IDENTIFICATION BY GLIADIN ELECTROPHOREGRAMS .1. APPARATUS, METHOD AND NOMENCLATURE [J].
BUSHUK, W ;
ZILLMAN, RR .
CANADIAN JOURNAL OF PLANT SCIENCE, 1978, 58 (02) :505-515
[9]   UV resonance Raman-selective amide vibrational enhancement: Quantitative methodology for determining protein secondary structure [J].
Chi, ZH ;
Chen, XG ;
Holtz, JSW ;
Asher, SA .
BIOCHEMISTRY, 1998, 37 (09) :2854-2864
[10]   Influence of different nitrogen application on flour properties, gluten properties by HPLC and end-use quality of Korean wheat [J].
Cho, Seong-Woo ;
Kang, Chon-Sik ;
Kang, Taek-Gyu ;
Cho, Kwang-Min ;
Park, Chul Soo .
JOURNAL OF INTEGRATIVE AGRICULTURE, 2018, 17 (05) :982-993