Dietary amino acid patterns and cardiometabolic risk factors among subjects with obesity; a cross-sectional study.

BACKGROUND: The prevalence of obesity is a growing global public health concern. Certain dietary amino acids have been shown to have a potential therapeutic role in improving metabolic syndrome parameters and body composition in individuals with obesity. However, some amino acids have been linked to an increased risk of cardiometabolic disorders. This cross-sectional study aims to investigate the association between dietary amino acid patterns and cardiometabolic risk factors in individuals with obesity. METHODS: This cross-sectional study included 335 participants with obesity (57.9% males and 41.5% females) from Tabriz and Tehran, Iran. The participants were between the ages of 20-50, with a body mass index (BMI) of 30 kg/m2 or higher, and free from certain medical conditions. The study examined participants' general characteristics, conducted anthropometric assessments, dietary assessments, and biochemical assessments. The study also used principal component analysis to identify amino acid intake patterns and determined the association between these patterns and cardiometabolic risk factors in individuals with obesity. RESULTS: Upon adjusting for potential confounders, the study found that individuals in the third tertiles of pattern 1 and 2 were more likely to have lower LDL levels (OR = 0.99 and 95% CI (0.98-0.99)) for both. Additionally, a significant decrease in total cholesterol was observed in the third tertiles of pattern 2 in model II (OR = 0.99, 95% CI (0.98-0.99)). These findings suggest a potential cardioprotective effect of these amino acid patterns in managing cardiometabolic risk factors in individuals with obesity. CONCLUSIONS: This study found that two identified amino acid patterns were associated with lower serum LDL and total cholesterol levels, while a third pattern was associated with higher serum triglycerides. The specific amino acids contributing to these patterns highlight the importance of targeted dietary interventions in managing cardiometabolic risk factors in individuals with obesity.

Development of a Comprehensive Quality Evaluation System for Foxtail Millet from Different Ecological Regions.

Foxtail millet (Setaria italica L.) is a critical grain with high nutritional value and the potential for increased production in arid and semiarid regions. The foxtail millet value chain can be upgraded only by ensuring its comprehensive quality. Thus, samples were collected from different production areas in Shanxi province, China, and compared in terms of quality traits. We established a quality evaluation system utilizing multivariate statistical analysis. The results showed that the appearance, nutritional content, and culinary value of foxtail millet produced in different ecological regions varied substantially. Different values of amino acids (DVAACs), alkali digestion values (ADVs), and total flavone content (TFC) had the highest coefficients of variation (CVs) of 50.30%, 39.75%, and 35.39%, respectively. Based on this, a comprehensive quality evaluation system for foxtail millet was established, and the quality of foxtail millet produced in the five production areas was ranked in order from highest to lowest: Dingxiang > Zezhou > Qinxian > Xingxian > Yuci. In conclusion, the ecological conditions of Xinding Basin are favorable for ensuring the comprehensive quality of foxtail millet. .

Ratio of Hydrophobic-Hydrophilic and Positive-Negative Residues at Lipid-Water-Interface Influences Surface Expression and Channel Gating of TRPV1.

During evolution, TRPV1 has lost, retained or selected certain residues at Lipid-Water-Interface (LWI) and formed specific patterns there. The ratio of "hydrophobic-hydrophilic" and "positive-negative-charged" residues at the inner LWI remains conserved throughout vertebrate evolution and plays important role in regulating TRPV1 trafficking and localization. Arg575 is an important residue as Arg575Asp mutant has reduced surface expression, co-localization with lipid raft markers, cell area and increased cell lethality. This lethality is most likely due to the disruption of the ratio between positive-negative charges caused by the mutation. Such lethality can be rescued by either using TRPV1-specfic inhibitor 5'-IRTX or by restoring the positive-negative charge ratio at that position, i.e. by introducing Asp576Arg mutation in Arg575Asp backbone. We propose that Arg575Asp mutation confers TRPV1 in a "constitutive-open-like" condition. These findings have broader implication in understanding the molecular evolution of thermo-sensitive ion channels and the micro-environments involved in processes that goes erratic in different diseases. The segment of TRPV1 that is present at the inner lipid-water-interface (LWI) has a specific pattern of amino acid combinations. The overall ratio of +ve charge /-ve charge and the ratio of hydrophobicity/hydrophilicity remain constant throughout the vertebrate evolution (ca 450 million years). This specific pattern is not observed in the outer LWI region of TRPV1.

Is the amino acid pattern in medical nutrition therapy crucial for successfully attenuating muscle mass loss in adult ICU patients? Secondary analysis of a RCT.

BACKGROUND AND AIMS: We hypothesized that in long-term immobilized intensive care unit (ICU) patients, both the quantity and quality of protein nutrition are vital in supporting muscle mass maintenance. Hence, the aim of this secondary analysis of our recently performed RCT was to calculate the intake of individual amino acids and to evaluate the potential associations of amino acid patterns with muscle mass loss during the ICU stay. METHODS: Clinical and nutritional data were collected from a recent RCT conducted in long-term immobilized, critically ill patients receiving medical nutrition therapy with either 1.8 g (interventional group) or 1.2 g (standard group) of protein/amino acids per kg body weight per day over 4 weeks. Intake of the individual amino acids as well as the sum scores of the indispensable, conditionally indispensable, and dispensable amino acids were calculated for all patients, both group specific (n = 21 in each group) and in total (n = 42), based on the detailed nutrition protocols; inter-group differences were analyzed by t-tests. Linear regression models were used to test the effects of individual amino acids and the sum scores on the extent of skeletal muscle loss by measuring the quadriceps muscle layer thickness during the study period. The significance level was adjusted for multiple testing according to the Bonferroni procedure (α = 0.002). RESULTS: In both groups, the proportion of indispensable amino acids was approximately 41% of the total exogenous protein supply, with the proportion of enteral administration slightly over 50%. The intake of conditionally indispensable amino acids (glutamine, tyrosine, cysteine, histidine, and arginine) accounted for 17% and 18% of the total amino acids in the interventional and standard groups, respectively; glutamine (5% of total amino acids) was exclusively administered enterally. The intake of dispensable amino acid varied widely, with glutamic acid, proline, and asparagine/aspartic acid representing the highest proportions (10%, 8%, and 8% of total amino acids, respectively). For all amino acids, no statistically significant association was observed between the quantitative intake and the skeletal muscle changes after terminating the intervention phase. CONCLUSION: This secondary analysis of the RCT conducted in routine clinical practice did not support our working hypothesis that the amino acid patterns of medical nutrition therapy have a statistically significant impact on the skeletal muscle loss in long-term immobilized ICU patients. Due to the limited variety of enteral/parenteral products used in this single-center study, the calculated amino acid patterns showed only small differences. Larger multi-center trials with adequate power are needed to evaluate the potential effects of the individual amino acids or defined amino acid patterns on the muscle protein metabolism in further detail. TRIAL REGISTRATION: German Clinical Trials Register (http://www.drks.de); DRKS-ID: DRKS00013594.

Conformational change following conversion of inactive rhinophrynin-33 to bioactive rhinophrynin-27 in the skin of the frog Rhinophrynus dorsalis.

Skin secretions of the Mexican burrowing toad Rhinophrynus dorsalis (Rhinophrynidae) contain the proline-arginine-rich peptide, rhinophrynin-27 (RP-27; ELRLPEIARPVPEVLPARLPLPALPRN) with insulinotropic and immunomodulatory properties, together with a higher concentration of the biologically inactive form, rhinophrynin-33 (RP-33) that constitutes RP-27 extended from its C-terminus by the hexapeptide KMAKNQ. Determination of the conformation of RP-33 by NMR demonstrates that in both water and in a solvent that promotes protein folding (50% trifluoroethanol-water), the majority of the proline residues are found in a polyproline type II helical region. The peptide adopts a horseshoe (U-shaped) conformation with pronounced bends in the molecule of around 100°-120° at Glu13 and Arg18. The hexapeptide extension adopts a α-helical conformation. When the hexapeptide is excised to generate RP-27, the molecule adopts an L-shaped conformation with a single bend at Glu13. A search of protein sequence databases indicated the P-X-P-XXX-P-XXX-P-X-P motif found in RP-27 and RP-33 occurs in a number of proteins although its functional implications are unclear. The data suggest that RP-33 represents a biosynthetic precursor of RP-27 that is activated by a protease cleaving at a single lysine residue of the type previously identified in Xenopus laevis skin secretions.

The Limiting Sequence and Appropriate Amino Acid Ratio of Lysine, Methionine, and Threonine for Seven- to Nine-Month-Old Holstein Heifers Fed Corn-Soybean M-Based Diet.

An "Amino acid (AA) partial deletion method" was used in this experiment to study the limiting sequences and appropriate ratio of lysine (Lys), methionine (Met), and threonine (Thr) in the diets of 7- to 9-month-old Holstein heifers. The experiment was conducted for three months with 72 Holstein heifers (age = 22 ± 0.5 weeks old; BW = 200 ± 9.0 kg; mean ± standard deviation). Following an initial two weeks adaptation period, heifers were allocated to one of four treatments: a theoretically balanced amino acid diet (positive control [PC]; 1.00% Lys, 0.33% Met, and 0.72% Thr), a 30% Lys deleted diet (partially deleted Lys [PD-Lys]; 0.66% Lys, 0.33% Met, and 0.72% Thr), a 30% Met deleted diet (partially deleted Met, [PD-Met]; 1.00% Lys, 0.22% Met, and 0.72% Thr), and a 30% Thr deleted diet (partially deleted Thr [PD-Thr]; 1.00% Lys, 0.33% Met, and 0.45% Thr). Experimental animals were fed a corn-soybean meal-based concentrate and alfalfa hay. In addition, the animals were provided with supplemental Lys, Met, and Thr (ruminal bypass). The results found no differences in the growth performance and nitrogen retention between PD-Thr treatment and PC treatment (p > 0.05). The average daily gain (p = 0.0013) and feed conversion efficiency (p = 0.0057) of eight- to ninr-month-old heifers were lower in both PD-Lys and PD-Met treatment than those in PC treatment. According to growth performance, Lys was the first limiting AA, followed by Met and Thr. Moreover, nine-month-old Holstein heifers in PD-Lys treatment and PD-Met treatment had higher levels of serum urea nitrogen (p = 0.0021), urea nitrogen (p = 0.0011) and total excreted N (p = 0.0324) than those in PC treatment, which showed that nitrogen retention significantly decreased (p = 0.0048) as dietary Lys and Met levels decreased. The limiting sequence based on nitrogen retention was the same as that based on growth performance. The appropriate ratio of Lys, Met, and Thr in the diet based on nitrogen retention was 100:32:57. In summary, the limiting sequence and appropriate amino acid ratio of Lys, Met, and Thr for seven- to nine-month-old Holstein heifers fed a corn-soybean meal-based diet were Lys > Met > Thr and 100:32:57, respectively.

50 years of amino acid hydrophobicity scales: revisiting the capacity for peptide classification.

BACKGROUND: Physicochemical properties are frequently analyzed to characterize protein-sequences of known and unknown function. Especially the hydrophobicity of amino acids is often used for structural prediction or for the detection of membrane associated or embedded ß-sheets and α-helices. For this purpose many scales classifying amino acids according to their physicochemical properties have been defined over the past decades. In parallel, several hydrophobicity parameters have been defined for calculation of peptide properties. We analyzed the performance of separating sequence pools using 98 hydrophobicity scales and five different hydrophobicity parameters, namely the overall hydrophobicity, the hydrophobic moment for detection of the α-helical and ß-sheet membrane segments, the alternating hydrophobicity and the exact ß-strand score. RESULTS: Most of the scales are capable of discriminating between transmembrane α-helices and transmembrane ß-sheets, but assignment of peptides to pools of soluble peptides of different secondary structures is not achieved at the same quality. The separation capacity as measure of the discrimination between different structural elements is best by using the five different hydrophobicity parameters, but addition of the alternating hydrophobicity does not provide a large benefit. An in silico evolutionary approach shows that scales have limitation in separation capacity with a maximal threshold of 0.6 in general. We observed that scales derived from the evolutionary approach performed best in separating the different peptide pools when values for arginine and tyrosine were largely distinct from the value of glutamate. Finally, the separation of secondary structure pools via hydrophobicity can be supported by specific detectable patterns of four amino acids. CONCLUSION: It could be assumed that the quality of separation capacity of a certain scale depends on the spacing of the hydrophobicity value of certain amino acids. Irrespective of the wealth of hydrophobicity scales a scale separating all different kinds of secondary structures or between soluble and transmembrane peptides does not exist reflecting that properties other than hydrophobicity affect secondary structure formation as well. Nevertheless, application of hydrophobicity scales allows distinguishing between peptides with transmembrane α-helices and ß-sheets. Furthermore, the overall separation capacity score of 0.6 using different hydrophobicity parameters could be assisted by pattern search on the protein sequence level for specific peptides with a length of four amino acids.

50 years of amino acid hydrophobicity scales: revisiting the capacity for peptide classification

BACKGROUND: Physicochemical properties are frequently analyzed to characterize protein-sequences of known and unknown function. Especially the hydrophobicity of amino acids is often used for structural prediction or for the detection of membrane associated or embedded ß-sheets and α-helices. For this purpose many scales classifying amino acids according to their physicochemical properties have been defined over the past decades. In parallel, several hydrophobicity parameters have been defined for calculation of peptide properties. We analyzed the performance of separating sequence pools using 98 hydrophobicity scales and five different hydrophobicity parameters, namely the overall hydrophobicity, the hydrophobic moment for detection of the α-helical and ß-sheet membrane segments, the alternating hydrophobicity and the exact ß-strand score. RESULTS: Most of the scales are capable of discriminating between transmembrane α-helices and transmembrane ß-sheets, but assignment of peptides to pools of soluble peptides of different secondary structures is not achieved at the same quality. The separation capacity as measure of the discrimination between different structural elements is best by using the five different hydrophobicity parameters, but addition of the alternating hydrophobicity does not provide a large benefit. An in silico evolutionary approach shows that scales have limitation in separation capacity with a maximal threshold of 0.6 in general. We observed that scales derived from the evolutionary approach performed best in separating the different peptide pools when values for arginine and tyrosine were largely distinct from the value of glutamate. Finally, the separation of secondary structure pools via hydrophobicity can be supported by specific detectable patterns of four amino acids. CONCLUSION: It could be assumed that the quality of separation capacity of a certain scale depends on the spacing of the hydrophobicity value of certain amino acids. Irrespective of the wealth of hydrophobicity scales a scale separating all different kinds of secondary structures or between soluble and transmembrane peptides does not exist reflecting that properties other than hydrophobicity affect secondary structure formation as well. Nevertheless, application of hydrophobicity scales allows distinguishing between peptides with transmembrane α-helices and ß-sheets. Furthermore, the overall separation capacity score of 0.6 using different hydrophobicity parameters could be assisted by pattern search on the protein sequence level for specific peptides with a length of four amino acids.

Glutamine synthetase activity in leaves of Zea mays L. as influenced by magnesium status.

MAIN CONCLUSION: The total capacity of the GS-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. Magnesium deficiency does not obligatorily lead to the decreased total protein concentrations in the leaves. Magnesium (Mg) is an integral component of the enzyme glutamine synthetase (GS), having both a structural and a catalytic role. Moreover, Mg is relevant for the post-translational regulation of the GS. Glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium (NH4 (+)) to glutamate to form glutamine and it is therefore crucial for plant growth and productivity. This study was conducted in order to test whether a severe Mg-deficiency impairs the total capacity of the GS-catalyzed synthesis of glutamine in maize leaves. Maize was grown hydroponically and the GS activity was analyzed dependent on different leaf developmental stages. Glutamine synthetase activity in vitro assays in combination with immune-dot blot analysis revealed that both the total activity and the abundance of glutamine synthetase was not impaired in the leaves of maize plants upon 54 days of severe Mg starvation. Additionally, it was shown that Mg deficiency does not obligatorily lead to decreased total protein concentrations in the leaves, as assayed by Bradford protein quantification. Moreover, Mg resupply to the roots or the leaves of Mg-deficient plants reversed the Mg-deficiency-induced accumulation of free amino acids in older leaves, which indicates impaired phloem loading. The results of our study reveal that the total GS-mediated primary or secondary assimilation of free NH4 (+) is not a limiting enzymatic reaction under Mg deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize.