scholarly journals Application of advanced synchrotron radiation-based Fourier transform infrared (SR-FTIR) microspectroscopy to animal nutrition and feed science: a novel approach

2004 ◽  
Vol 92 (6) ◽  
pp. 869-885 ◽  
Author(s):  
P. Yu
Keyword(s):  
Animal Nutrition ◽  
Starch Granules ◽  
Endosperm Tissue ◽  
Rumen Degradation ◽  
Novel Approach ◽  
Nutrient Utilisation ◽  
Ftir Technique ◽  
Feed Protein ◽  
Α Helix ◽  
Β Sheet

Synchrotron radiation-based Fourier transform IR (SR-FTIR) microspectroscopy has been developed as a rapid, direct, non-destructive and bioanalytical technique. This technique, taking advantage of synchrotron light brightness and a small effective source size, is capable of exploring the molecular chemistry within the microstructures of a biological tissue without the destruction of inherent structures at ultraspatial resolutions within cellular dimensions. This is in contrast to traditional ‘wet’ chemical methods, which, during processing for analysis, often result in the destruction of the intrinsic structures of feeds. To date there has been very little application of this technique to the study of feed materials in relation to animal nutrient utilisation. The present article reviews four applications of the SR-FTIR bioanalytical technique as a novel approach in animal nutrition and feed science research. Application 1 showed that using the SR-FTIR technique, intensities and the distribution of the biological components (such as lignin, protein, lipid, structural and non-structural carbohydrates and their ratios) in the microstructure of plant tissue within cellular dimensions could be imaged. The implication from this study is that we can chemically define the intrinsic feed structure and compare feed tissues according to spectroscopic characteristics, functional groups, spatial distribution and chemical intensity. Application 2 showed that the ultrastructural–chemical makeup and density of yellow- and brown-seeded Brassica rape could be explored. This structural–chemical information could be used for the prediction of rapeseed quality and nutritive value for man and animals and for rapeseed breeding programmes for selecting superior varieties for special purposes. More research is required to define the extent of differences that exist between the yellow- and brown-seeded Brassica rape. Application 3 showed with the SR-FTIR technique that chemical differences in the ultrastructural matrix of endosperm tissue between Harrington (malting-type) and Valier (feed-type) barley in relation to rumen degradation characteristics could be identified. The results indicated that the greater association of the protein matrix with the starch granules in the endosperm tissue of Valier barley may limit the access of ruminal micro-organisms to the starch granules and thus reduce the rate and extent of rumen degradation relative to that of Harrington barley. It is the first time that the microstructural matrix in the endosperm of barley has been revealed by using the SR-FTIR technique, which makes it possible to link feed intrinsic structures to nutrient utilisation and digestive behaviour in ruminants. Application 4 showed with the SR-FTIR technique that the chemical features of various feed protein (amide I) secondary structures (such as feather, wheat, oats and barley) could be quantified. With a multi-component fitting program (Lorentz function), the results showed feather containing about 88% β-sheet and 4% α-helix, barley containing about 17% β-sheet and 71% α-helix; oats containing about 2% β-sheet and 92% α-helix; and wheat containing about 42% β-sheet and 50% α-helix. The relative percentage of the two may influence protein value. A high percentage of β-sheet may reduce the access of gastrointestinal digestive enzymes to the protein structure. Further study is required on feed protein secondary structures in relation to enzyme accessibility and digestibility. In conclusion, the SR-FTIR technique can be used for feed science and animal nutrition research. However, the main disadvantage of this technique is the requirement for a special light source; a synchrotron beam.

Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: A novel approach

2005 ◽  
Vol 85 (4) ◽  
pp. 437-448 ◽  
Author(s):  
P. Yu ◽  
J. J. McKinnon ◽  
H. W. Soita ◽  
C. R. Christensen ◽  
D. A. Christensen
Keyword(s):  
Secondary Structure ◽  
Matrix Protein ◽  
Protein Secondary Structure ◽  
Secondary Structures ◽  
Heat Processing ◽  
Lower Percentage ◽  
Protein Secondary Structures ◽  
Novel Approach ◽  
Α Helix ◽  
Β Sheet

The objectives of the study were to use synchrotron Fourier transform infrared microspectroscopy (S-FTIR) as a novel approach to: (1) reveal ultra-structural chemical features of protein secondary structures of flaxseed tissues affected by variety (golden and brown) and heat processing (raw and roasted), and (2) quantify protein secondary structures using Gaussian and Lorentzian methods of multi-component peak modeling. By using multi-component peak modeling at protein amide I region of 1700–1620 cm-1, the results showed that the golden flaxseed contained relatively higher percentage of α-helix (47.1 vs. 36.9%), lower percentage of β-sheet (37.2 vs. 46.3%) and higher (P < 0.05) ratio of α-helix to β-sheet than the brown flaxseed (1.3 vs. 0.8). The roasting reduced (P < 0.05) percentage of α-helix (from 47.1 to 36.1%), increased percentage of β-sheet (from 37.2 to 49.8%) and reduced α-helix to β-sheet ratio (1.3 to 0.7) of the golden flaxseed tissues. However, the roasting did not affect percentage and ratio of α-helix and β-sheet in the brown flaxseed tissue. No significant differences were found in quantification of protein secondary structures between Gaussian and Lorentzian methods. These results demonstrate the potential of highly spatially resolved S-FTIR to localize relatively pure protein in the tissue and reveal protein secondary structures at a cellular level. The results indicated relative differences in protein secondary structures between flaxseed varieties and differences in sensitivities of protein secondary structure to the heat processing. Further study is needed to understand the relationship between protein secondary structure and protein digestion and utilization of flaxseed and to investigate whether the changes in the relative amounts of protein secondary structures are primarily responsible for differences in protein availability. Key words: Synchrotron, FTIR microspectrosopy, flaxseeds, intrinsic structural matrix, protein secondary structures, protein nutritive value

scholarly journals Relationship of protein molecular structure to metabolisable proteins in different types of dried distillers grains with solubles: a novel approach

2010 ◽  
Vol 104 (10) ◽  
pp. 1429-1437 ◽  
Author(s):  
Peiqiang Yu ◽  
Waldo G. Nuez-Ortín
Keyword(s):  
Molecular Structure ◽  
Degradation Kinetics ◽  
Molecular Structures ◽  
Protein Balance ◽  
Rumen Degradation ◽  
Different Types ◽  
Α Helix ◽  
Protein Supply ◽  
Β Sheet ◽  
Intestinal Digestibility

To date, there has been no study of protein molecular structures affected by bioethanol processing in relation to protein nutritive values of the new co-products of bioethanol production. The objective of the present study was to investigate the relationship between protein molecular structures (in terms of protein α-helix and β-sheet spectral intensity and their ratio and amide I to amide II spectral intensity and their ratio) and protein rumen degradation kinetics (rate and extent), estimated protein intestinal digestibility and total truly absorbed protein in small intestine (metabolisable protein) in different types of dried distillers grains with solubles (DDGS), such as wheat DDGS, maize DDGS and blend DDGS (wheat:maize = 70:30). The protein molecular structures of the different types of DDGS affected by processing were identified using diffuse reflectance IR Fourier transform spectroscopy. The results showed that the protein structure α-helix to β-sheet ratio in the DDGS had a strongly negative correlation with estimated intestinal digestibility of ruminally undegraded protein (%dRUP, R − 0·95, P = 0·04), tended to have a significant correlation with the protein PC subfraction (which was undegradable and contained proteins associated with lignin and tannins and heat-damaged proteins) (R 0·91, P = 0·09) and had no correlation (P>0·10) with rumen degradation kinetics (rate and extent), total intestinally absorbed protein supply and degraded protein balance. However, the protein amide I to amide II ratio in the DDGS had a strongly positive correlation with soluble crude protein (CP) (R 0·99, P < 0·01), protein PA subfraction (which was instantaneously solubilised at time zero) (R 0·99, P < 0·01), protein PB2 subfraction (which was intermediately degradable) (R − 0·95, P = 0·04) and total digestible CP (R 0·95, P = 0·04). The amide I to amide II ratio also had strongly negative correlations with ruminally undegraded protein (%RUP: R − 0·96, P = 0·03) and the degraded protein balance (OEB: R − 0·97, P = 0·02), but had no correlation (P>0·10) with the total intestinally absorbed protein supply. Multiple regression results show that the protein structure α-helix to β-sheet ratio was a better predictor of %dRUP with R2 0·92. The amide I to II ratio was a better predictor of the degraded protein balance with R2 0·93 in the DDGS. In conclusion, the changes in the protein molecular structure α-helix to β-sheet ratio and the amide I to amide II ratio during bioethanol processing (either due to fermentation processing or due to heat drying) were highly associated with estimated protein intestinal digestibility and degraded protein balance, but were not associated with total intestinally absorbed protein supply from the DDGS to dairy cattle. The present study indicates that a potential novel method could be developed based on the protein molecular structure parameters to improve the estimation of protein value after a validation in a large-scale in vivo study is done.

scholarly journals Use of synchrotron FTIR microspectroscopy to identify chemical differences in barley endosperm tissue in relation to rumen degradation characteristics

2004 ◽  
Vol 84 (3) ◽  
pp. 523-527 ◽  
Author(s):  
P. Yu ◽  
D. A. Christensen ◽  
C. R. Christensen ◽  
M. D. Drew ◽  
B. G. Rossnagel ◽  
...  
Keyword(s):  
Signal To Noise Ratio ◽  
Close Association ◽  
Intact Plant ◽  
High Rate ◽  
High Signal ◽  
Starch Granules ◽  
Endosperm Tissue ◽  
Rumen Degradation ◽  
Infrared Microspectroscopy ◽  
Ftir Microspectroscopy

Valier (feed-type) and Harrington (malting-type) barley differ in rumen degradation characteristics. Harrington, in contrasts to Valier, exhibits a high rate and extent of rumen degradation, which can lead to metabolic problems such as acidosis and bloat in ruminants. Traditional “wet” chemical analysis cannot detect biological differences between barley varieties due to destruction of endosperm structure during processing. Synchrotron Fourier transform infrared microspectroscopy (SR-FTIR) is capable of exploring the chemical makeup of intact plant tissue with high signal to noise ratio at spatial resolutions as fine as 3~10 µm. The objective of this study was to use SR-FTIR microspectroscopy to explore and identify chemical differences in the ultra-structural matrix of the endosperm tissue of the two barley varieties as related to differences in rumen degradation characteristics. The results showed that the infrared absorbance intensity (Log 1/R) of the starch and protein varied considerably between the two varieties, but were not statistically significant. Harrington had a wider range of starch to protein IR absorbance intensity ratio (1.406 to 10.119 vs. 1.419 to 4.274), suggesting that it is more heterogeneous than Valier in endosperm chemical makeup. Valier had a lower ratio of starch to protein IR absorbance intensity than Harrington (P < 0.05), which implies that the starch granules in Valier are more closely associated with the protein matrix. This close association may prevent the starch granules from being rapidly degraded in the rumen. This work shows that the chemical makeup of intact plant tissues can be carried out by SR-FTIR microspectroscopy at ultra-spatial resolution (10 × 10 µm). Key words: Synchrotron infrared microspectroscopy, feed chemistry, barley, rumen degradability

Scorpion toxin-potassium channel interaction law and its applications.

2020 ◽  
Vol 01 ◽  
Author(s):  
Zheng Zuo ◽  
Zongyun Chen ◽  
Zhijian Cao ◽  
Wenxin Li ◽  
Yingliang Wu
Keyword(s):  
Potassium Channel ◽  
Scorpion Toxin ◽  
Scorpion Toxins ◽  
Toxin Binding ◽  
Channel Interaction ◽  
Binding Interface ◽  
Α Helix ◽  
Interaction Law ◽  
Binding Interfaces ◽  
Β Sheet

: The scorpion toxins are the largest potassium channel-blocking peptide family. The understanding of toxin binding interfaces is usually restricted by two classical binding interfaces: one is the toxin α-helix motif, the other is the antiparallel β-sheet motif. In this review, such traditional knowledge was updated by another two different binding interfaces: one is BmKTX toxin using the turn motif between the α-helix and antiparallel β-sheet domains as the binding interface, the other is Ts toxin using turn motif between the β-sheet in the N-terminal and α-helix domains as the binding interface. Their interaction analysis indicated that the scarce negatively charged residues in the scorpion toxins played a critical role in orientating the toxin binding interface. In view of the toxin negatively charged amino acids as “binding interface regulator”, the law of scorpion toxin-potassium channel interaction was proposed, that is, the polymorphism of negatively charged residue distribution determines the diversity of toxin binding interfaces. Such law was used to develop scorpion toxin-potassium channel recognition control technique. According to this technique, three Kv1.3 channel-targeted peptides, using BmKTX as the template, were designed with the distinct binding interfaces from that of BmKTX through modulating the distribution of toxin negatively charged residues. In view of the potassium channel as the common targets of different animal toxins, the proposed law was also shown to helpfully orientate the binding interfaces of other animal toxins. Clearly, the toxin-potassium channel interaction law would strongly accelerate the research and development of different potassium channelblocking animal toxins in the future.

scholarly journals Nanostructure of bioactive glass affects bone cell attachment via protein restructuring upon adsorption

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ukrit Thamma ◽  
Tia J. Kowal ◽  
Matthias M. Falk ◽  
Himanshu Jain
Keyword(s):  
Bioactive Glass ◽  
Cell Response ◽  
Interfacial Layer ◽  
Cell Attachment ◽  
Bone Cell ◽  
Nano Structure ◽  
Rgd Sequence ◽  
Engineered Tissue ◽  
Α Helix ◽  
Β Sheet

AbstractThe nanostructure of engineered bioscaffolds has a profound impact on cell response, yet its understanding remains incomplete as cells interact with a highly complex interfacial layer rather than the material itself. For bioactive glass scaffolds, this layer comprises of silica gel, hydroxyapatite (HA)/carbonated hydroxyapatite (CHA), and absorbed proteins—all in varying micro/nano structure, composition, and concentration. Here, we examined the response of MC3T3-E1 pre-osteoblast cells to 30 mol% CaO–70 mol% SiO2 porous bioactive glass monoliths that differed only in nanopore size (6–44 nm) yet resulted in the formation of HA/CHA layers with significantly different microstructures. We report that cell response, as quantified by cell attachment and morphology, does not correlate with nanopore size, nor HA/CHO layer micro/nano morphology, or absorbed protein amount (bovine serum albumin, BSA), but with BSA’s secondary conformation as indicated by its β-sheet/α-helix ratio. Our results suggest that the β-sheet structure in BSA interacts electrostatically with the HA/CHA interfacial layer and activates the RGD sequence of absorbed adhesion proteins, such as fibronectin and vitronectin, thus significantly enhancing the attachment of cells. These findings provide new insight into the interaction of cells with the scaffolds’ interfacial layer, which is vital for the continued development of engineered tissue scaffolds.

scholarly journals Structural and Technological Approach to Reveal the Role of the Lipid Phase in the Formation of Soy Emulsion Gels with Chia Oil

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 48
Author(s):  
Ana M. Herrero ◽  
Claudia Ruiz-Capillas
Keyword(s):  
Raman Spectroscopy ◽  
Structural Properties ◽  
Structural Changes ◽  
Protein Secondary Structure ◽  
Lipid Phase ◽  
Α Helix ◽  
Β Sheet ◽  
Shed Light ◽  
Chia Oil

Considerable attention has been paid to emulsion gels (EGs) in recent years due to their interesting applications in food. The aim of this work is to shed light on the role played by chia oil in the technological and structural properties of EGs made from soy protein isolates (SPI) and alginate. Two systems were studied: oil-free SPI gels (SPI/G) and the corresponding SPI EGs (SPI/EG) that contain chia oil. The proximate composition, technological properties (syneresis, pH, color and texture) and structural properties using Raman spectroscopy were determined for SPI/G and SPI/EG. No noticeable (p > 0.05) syneresis was observed in either sample. The pH values were similar (p > 0.05) for SPI/G and SPI/EG, but their texture and color differed significantly depending on the presence of chia oil. SPI/EG featured significantly lower redness and more lightness and yellowness and exhibited greater puncture and gel strengths than SPI/G. Raman spectroscopy revealed significant changes in the protein secondary structure, i.e., higher (p < 0.05) α-helix and lower (p < 0.05) β-sheet, turn and unordered structures, after the incorporation of chia oil to form the corresponding SPI/EG. Apparently, there is a correlation between these structural changes and the textural modifications observed.

scholarly journals Assessment of Amyloid Forming Tendency of Peptide Sequences from Amyloid Beta and Tau Proteins Using Force-Field, Semi-Empirical, and Density Functional Theory Calculations

2021 ◽  
Vol 22 (6) ◽  
pp. 3244
Author(s):  
Charuvaka Muvva ◽  
Natarajan Arul Murugan ◽  
Venkatesan Subramanian
Keyword(s):  
Force Field ◽  
Density Functional ◽  
Amyloid Β ◽  
Density Functional Theory Calculations ◽  
Tau Proteins ◽  
Functional Theory ◽  
Energy Profiles ◽  
Α Helix ◽  
Semi Empirical ◽  
Β Sheet

A wide variety of neurodegenerative diseases are characterized by the accumulation of protein aggregates in intraneuronal or extraneuronal brain regions. In Alzheimer’s disease (AD), the extracellular aggregates originate from amyloid-β proteins, while the intracellular aggregates are formed from microtubule-binding tau proteins. The amyloid forming peptide sequences in the amyloid-β peptides and tau proteins are responsible for aggregate formation. Experimental studies have until the date reported many of such amyloid forming peptide sequences in different proteins, however, there is still limited molecular level understanding about their tendency to form aggregates. In this study, we employed umbrella sampling simulations and subsequent electronic structure theory calculations in order to estimate the energy profiles for interconversion of the helix to β-sheet like secondary structures of sequences from amyloid-β protein (KLVFFA) and tau protein (QVEVKSEKLD and VQIVYKPVD). The study also included a poly-alanine sequence as a reference system. The calculated force-field based free energy profiles predicted a flat minimum for monomers of sequences from amyloid and tau proteins corresponding to an α-helix like secondary structure. For the parallel and anti-parallel dimer of KLVFFA, double well potentials were obtained with the minima corresponding to α-helix and β-sheet like secondary structures. A similar double well-like potential has been found for dimeric forms for the sequences from tau fibril. Complementary semi-empirical and density functional theory calculations displayed similar trends, validating the force-field based free energy profiles obtained for these systems.

Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix 1 1Edited by C. R. Matthews

2000 ◽  
Vol 296 (4) ◽  
pp. 1039-1051 ◽  
Author(s):  
Vincent Forge ◽  
Masaru Hoshino ◽  
Kazuo Kuwata ◽  
Munehito Arai ◽  
Kunihiro Kuwajima ◽  
...  
Keyword(s):  
Α Helix ◽  
Β Lactoglobulin ◽  
Β Sheet

scholarly journals Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach

2005 ◽  
Vol 94 (5) ◽  
pp. 655-665 ◽  
Author(s):  
Peiqiang Yu
Keyword(s):  
Nutritive Value ◽  
Secondary Structures ◽  
Cellular Level ◽  
Heat Processing ◽  
Molecular Chemistry ◽  
New Approach ◽  
Ftir Microspectroscopy ◽  
Protein Secondary Structures ◽  
Α Helix ◽  
Β Sheet

Studying the secondary structure of proteins leads to an understanding of the components that make up a whole protein, and such an understanding of the structure of the whole protein is often vital to understanding its digestive behaviour and nutritive value in animals. The main protein secondary structures are the α-helix and β-sheet. The percentage of these two structures in protein secondary structures influences protein nutritive value, quality and digestive behaviour. A high percentage of β-sheet structure may partly cause a low access to gastrointestinal digestive enzymes, which results in a low protein value. The objectives of the present study were to use advanced synchrotron-based Fourier transform IR (S-FTIR) microspectroscopy as a new approach to reveal the molecular chemistry of the protein secondary structures of feed tissues affected by heat-processing within intact tissue at a cellular level, and to quantify protein secondary structures using multicomponent peak modelling Gaussian and Lorentzian methods, in relation to protein digestive behaviours and nutritive value in the rumen, which was determined using the Cornell Net Carbohydrate Protein System. The synchrotron-based molecular chemistry research experiment was performed at the National Synchrotron Light Source at Brookhaven National Laboratory, US Department of Energy. The results showed that, with S-FTIR microspectroscopy, the molecular chemistry, ultrastructural chemical make-up and nutritive characteristics could be revealed at a high ultraspatial resolution (∼10 μm). S-FTIR microspectroscopy revealed that the secondary structure of protein differed between raw and roasted golden flaxseeds in terms of the percentages and ratio of α-helixes and β-sheets in the mid-IR range at the cellular level. By using multicomponent peak modelling, the results show that the roasting reduced (P<0·05) the percentage of α-helixes (from 47·1 % to 36·1 %: S-FTIR absorption intensity), increased the percentage of β-sheets (from 37·2 % to 49·8 %: S-FTIR absorption intensity) and reduced the α-helix to β-sheet ratio (from 0·3 to 0·7) in the golden flaxseeds, which indicated a negative effect of the roasting on protein values, utilisation and bioavailability. These results were proved by the Cornell Net Carbohydrate Protein System in situ animal trial, which also revealed that roasting increased the amount of protein bound to lignin, and well as of the Maillard reaction protein (both of which are poorly used by ruminants), and increased the level of indigestible and undegradable protein in ruminants. The present results demonstrate the potential of highly spatially resolved synchrotron-based infrared microspectroscopy to locate ‘pure’ protein in feed tissues, and reveal protein secondary structures and digestive behaviour, making a significant step forward in and an important contribution to protein nutritional research. Further study is needed to determine the sensitivities of protein secondary structures to various heat-processing conditions, and to quantify the relationship between protein secondary structures and the nutrient availability and digestive behaviour of various protein sources. Information from the present study arising from the synchrotron-based IR probing of the protein secondary structures of protein sources at the cellular level will be valuable as a guide to maintaining protein quality and predicting digestive behaviours.

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