Types Of Amino Acids Research Articles

Gas aggregated Ag NPs as a matrix for small molecules: a study on natural amino acids

The use of nanomaterials as a matrix for soft ionization mass spectrometry has been investigated and reported various times. Under certain conditions, measurements of samples containing small molecules enhanced by nanomaterials have better sensitivity compared with other methods. Nanoscaled Ag prepared by various methods was reported as a substrate for surface-assisted LDI MS. Higher desorption and (in some cases) charge transfer through adduct formation with silver ion was reported. But primary ionization mechanism was through attachment of proton or alkali ion. Our approach is to overcoat the sample by Ag nanoparticles (the so-called nanoparticle-assisted LDI MS or nanoPALDI MS). As nanoparticles having adsorption maxima close to the laser wavelength, we expect an improvement in desorption enhancement, release of silver ions and (as a result of latter) increased adduct formation of [analyte+Ag]+ ions. The nanoparticles are produced by gas aggregation under low-pressure, making the process homogeneous over relatively large areas, free from impurities, and absence of capping agent often presented in colloidal nanoparticles. This work reports the detection of natural amino acids with Ag nanoparticles as a matrix. We successfully detected all amino acids (as [analyte+Ag]+ ion), including in the mixtures of few amino acids. Moreover, a formation of other adducts, particularly [analyte+Ag3]+ and [analyte2+Ag]+ is reported. The differences in ion intensity ratios depending on amino acid types are discussed. The obtained results showed that laser ablation is more efficient for amino acids with hydrophobic, unique, and neutral side chains.

Metagenomic and Metatranscriptomic Analyses Revealed Uncultured Bacteroidales Populations as the Dominant Proteolytic Amino Acid Degraders in Anaerobic Digesters.

Current understanding of amino acid (AA) degraders in anaerobic digesters is mainly based on cultured species, whereas microorganisms that play important roles in a complex microbial community remain poorly characterized. This study investigated short-term enrichments degrading single AAs using metagenomics and metatranscriptomics. Metagenomic analysis revealed that populations related to cultured AA degraders had an abundance <2.5% of the sequences. In contrast, metagenomic-assembled bins related to uncultured Bacteroidales collectively accounted for >35% of the sequences. Phylogenetic analyses suggested that these Bacteroidales populations represented a yet-to-be characterized family lineage, i.e., Bacteroidetes vadinHA17. The bins possessed the genetic capacity related to protein degradation, including surface adhesion (3–7 genes), secreted peptidase (52–77 genes), and polypeptide-specific transporters (2–5 genes). Furthermore, metatranscriptomics revealed that these Bacteroidales populations expressed the complete metabolic pathways for degrading 16 to 17 types of AAs in enrichments fed with respective substrates. These characteristics were distinct from cultured AA degraders including Acidaminobacter and Peptoclostridium, suggesting the uncultured Bacteroidales were the major protein-hydrolyzing and AA-degrading populations. These uncultured Bacteroidales were further found to be dominant and active in full-scale anaerobic digesters, indicating their important ecological roles in the native habitats. “Candidatus Aminobacteroidaceae” was proposed to represent the previously uncharted family Bacteroidetes vadinHA17.

Synthesis of Nano-Hydroxyapatite of Different Morphologies and Their Cellular Compatibility

Nano-hydroxyapatite crystals of different morphologies were synthesized by adding two types of amino acids (glycine and arginine) under hydrothermal conditions. The XRD, FTIR, and TEM characterizations of samples showed that the final product was pure hydroxyapatite with high crystallinity. Organic small-molecule amino acids exhibited a significant inhibitory effect on crystal growth during the synthesis process. This regulatory effect is related to the side chains of amino acids. The results of co-culturing with bone mesenchymal stem cells showed that the cell compatibility of nanoparticles differs based on their morphologies. The results of this study are significant for the fabrication of nano-hydroxyapatite with tunable morphology, which can have applications in the fields of bone repair and drug loading.

Substitution scoring matrices for proteins - An overview.

Sequence analysis is the primary and simplest approach to discover structural, functional and evolutionary details of related proteins. All the alignment based approaches of sequence analysis make use of amino acid substitution matrices, and the accuracy of the results largely depends on the type of scoring matrices used to perform alignment tasks. An amino acid substitution matrix is a 20 × 20 matrix in which the individual elements encapsulate the rates at which each of the 20 amino acid residues in proteins are substituted by other amino acid residues over time. In contrast to most globular/ordered proteins whose amino acids composition is considered as standard, there are several classes of proteins (e.g., transmembrane proteins) in which certain types of amino acid (e.g., hydrophobic residues) are enriched. These compositional differences among various classes of proteins are manifested in their underlying residue substitution frequencies. Therefore, each of the compositionally distinct class of proteins or protein segments should be studied using specific scoring matrices that reflect their distinct residue substitution pattern. In this review, we describe the development and application of various substitution scoring matrices peculiar to proteins with standard and biased compositions. Along with most commonly used standard matrices (PAM, BLOSUM, MD and VTML) that act as default parameters in various homologs search and alignment tools, different substitution scoring matrices specific to compositionally distinct class of proteins are discussed in detail.

Effect of storage time on biochemical characteristics and antioxidant activity of hawk tea (Litsea coreana) processed by boiling water fixation.

This study investigated the effect of storage time on biochemical characteristics of hawk tea (Litsea coreana) and explored the correlation between the content of flavonoids and polyphenols and antioxidant activity. The antioxidant activity and the content of inclusions, amino acid, and mineral elements in hawk tea processed by boiling water fixation and packed in airtight polypropylene bags and stored in 0°C refrigerator under different storage time (one year, three years, and six years) were analyzed. Results indicated that the biochemical characteristics of hawk tea changed less within 12 months. The total content and types of amino acids in hawk tea reached the maximum in the third year, as well as the content of total trace elements. The water extracts, tea polyphenol, caffeine, lysine, valine, isoleucine, glycine, proline, Ca, and Zn decreased continuously in the storage period of 6 years, but the total flavonoids, Mg, and Ni changed just the opposite. Total polyphenol is the main antioxidant material in hawk tea. Results of the present study provided useful information for people to systematically understand the changes of tea in the storage process and to reasonably develop hawk tea product.

The relationship between protein domains and homopeptides in the Plasmodium falciparum proteome.

The proteome of the malaria parasite Plasmodium falciparum is notable for the pervasive occurrence of homopeptides or low-complexity regions (i.e., regions that are made from a small subset of amino-acid residue types). The most prevalent of these are made from residues encoded by adenine/thymidine (AT)-rich codons, in particular asparagine. We examined homopeptide occurrences within protein domains in P. falciparum. Homopeptide enrichments occur for hydrophobic (e.g., valine), or small residues (alanine or glycine) in short spans (<5 residues), but these enrichments disappear for longer lengths. We observe that short asparagine homopeptides (<10 residues long) have a dramatic relative depletion inside protein domains, indicating some selective constraint to keep them from forming. We surmise that this is possibly linked to co-translational protein folding, although there are specific protein domains that are enriched in longer asparagine homopeptides (≥10 residues) indicating a functional linkage for specific poly-asparagine tracts. Top gene ontology functional category enrichments for homopeptides associated with diverse protein domains include “vesicle-mediated transport”, and “DNA-directed 5′-3′ RNA polymerase activity”, with various categories linked to “binding” evidencing significant homopeptide depletions. Also, in general homopeptides are substantially enriched in the parts of protein domains that are near/in IDRs. The implications of these findings are discussed.

Molecular Docking Analysis of Chloroquine and Hydroxychloroquine and Design of Anti-SARS-CoV2 Protease Inhibitor

In this present investigation, simulated molecular docking study of chloroquine and hydroxychloroquine compounds were investigated on the SARS-CoV2 enzyme to determine the types of amino acids responsible for the biochemical reaction at the binding site. A structure-based docking design technique was explored in designing a novel derivative of chloroquine for the treatment and management of new COVID 19 disease. To achieve this, the molecular docking simulation method was used to investigate the level of chloroquine and hydroxychloroquine (Drugs presently under clinical trial) interactions on SARS-CoV2 enzyme (a causative agent of COVID 19 disease). Chloroquine and hydroxychloroquine which has been debated as drugs for the management of COVID 19 were subjected to molecular docking analysis, and the binding energies generated were found to be -6.1 kcal/mol and -6.8 kcal/mol respectively. Moreover, novel 2-((4-((7-chloroquinolin-4 yl) amino)pentyl)((methylamino)methyl)amino) ethan-1-ol as an anti-SARS-CoV2 protease was designed through the structural modification of hydroxychloroquine. The binding energy of this drug candidate was found to be -6.9 kcal/mol. This novel drug was found to formed hydrogen and conventional interactions with the binding site of SARS-CoV2 protease through amino acids such as Glutamic acid (GLU166), Glycine (GLY143), Phenylalanine (PHE140), Asparagine (ASN142), Histidine (HIS163), His (HIS172, HIS41, HIS163), Leucine (LEU41, LEU27), Glycine (GLY143), Glutamine (GLN189), Methionine (MET49, MET165), Serine (SER 46), Cysteine (CYS145) and Threonine (THR25). With this binding energy, this new drug candidate could bind better to the human SARS-CoV2 protease&amp;rsquo; binding site. This research provides a clue for other scientists on various ways of designing and identify the types of amino acids that may be responsible for biochemical action on SARS-CoV2 protease.

Substrate specificities of inteins investigated by QuickDrop-cassette mutagenesis.

Inteins catalyze self-excision from host precursor proteins while concomitantly ligating the flanking substrates (exteins) with a peptide bond. Noncatalytic extein residues near the splice junctions, such as the residues at the -1 and +2 positions, often strongly influence the protein-splicing efficiency. The substrate specificities of inteins have not been studied for many inteins. We developed a convenient mutagenesis platform termed "QuickDrop"-cassette mutagenesis for investigating the influences of 20 amino acid types at the -1 and +2 positions of different inteins. We elucidated 17 different profiles of the 20 amino acid dependencies across different inteins. The substrate specificities will accelerate our understanding of the structure-function relationship at the splicing junctions for broader applications of inteins in biotechnology and molecular biosciences.

Plasma amino acid pools in the umbilical cord artery show lower 15N natural isotope abundance relative to the maternal venous pools

ABSTRACT 15N natural isotope abundance (NIA) is systematically higher in infants’ hair than in that of their mothers at birth. This study aimed to investigate this difference in plasma pools. We compared 15N NIA values for plasma amino acid (AA) pools (free + protein-bound) in the umbilical cord artery (UCA) and vein (UCV) and in the maternal vein (MV) at birth. This preliminary study included 7 mother–infant dyads. Whole plasma was treated (HCl) to hydrolyze protein. Following derivatization, AAs were separated using gas chromatography and compound-specific 15N NIA values were measured on-line using an isotope ratio monitoring mass spectrometer. 15N NIA plasma AA pools in the UCA and UCV were highly correlated to the MV, r 2 > 0.89 and r 2 > 0.88 (both P < 10−4) respectively. The full model found a significant effect of sampling compartment (P = 0.02) and AA type (P < 0.0001) on 15N NIA plasma AA values. 15N NIA plasma AA was 0.74 ‰ higher (P = 0.01) in the MV than in the UCA. This study indicates that a decrease in 15N NIA for plasma AA pools occurs in the fetal–placental unit. Trial registration: ClinicalTrials.gov identifier: NCT00607061.

Entropy of Proteins Using Multiscale Cell Correlation.

A new multiscale method is presented to calculate the entropy of proteins from molecular dynamics simulations. Termed Multiscale Cell Correlation (MCC), the method decomposes the protein into sets of rigid-body units based on their covalent-bond connectivity at three levels of hierarchy: molecule, residue, and united atom. It evaluates the vibrational and topographical entropy from forces, torques, and dihedrals at each level, taking into account correlations between sets of constituent units that together make up a larger unit at the coarser length scale. MCC gives entropies in close agreement with normal-mode analysis and smaller than those using quasiharmonic analysis as well as providing much faster convergence. Moreover, MCC provides an insightful decomposition of entropy at each length scale and for each type of amino acid according to their solvent exposure and whether they are terminal residues. While the residue entropy depends weakly on solvent exposure, there is greater variation in entropy components for larger, more polar amino acids, which have increased conformational entropy but reduced vibrational entropy with greater solvent exposure.

OPTIMIZATION OF AMINO ACID PRODUCTION FROM CHICKEN FEATHER BY BACILLUS AMYLOLIQUEFACIENS USING RESPONSE SURFACE METHODOLOGY AS A NEW TOOL FOR POWDERY MILDEW DISEASE BIOCONTROL

The present work aimed to optimize amino acids production by Bacillus amyloliquefaciens 35s from chicken feather using response surface methodology (RSM) and applying the produced amino acids in biological control of powdery mildew disease. Variables affecting amino acids production from B. amyloliquefaciens 35s were screened using Plackett Burman design. Factors showed to be significant to produce amino acids were optimized using central composite design (CCD) of RSM at three coded levels (-1, 0, +1). All obtained data were analyzed by ANOVA with post hoc multiple comparison analysis performed using Tukey’s HSD. TGY (tryptone, glucose, yeast extract) was the basal medium. Impacts of medium components were studied using Plackett-Burman design. “Design Expert 12” StateEase was used to analyze the experimental Plackett- Burman design. Feather, yeast extract, CaCO3, KH2PO4 and agitation rate (using shake flask) were optimized statistically by the CCD design of the RSM. Validation of statistical model of the medium components was done by carrying out the experiment at optimum conditions of the process parameters as determined by the model. Amino acids types were identified by amino acid analyzer. Among the significant medium components, feather, yeast extract, CaCO3, KH2PO4 and agitation rate showed to have significant effect on amino acids production. Predicted maximum amino acids production was observed near the mid-point concentrations of the mentioned above factors and the experimental value (6.55 g/l) was very close to the predicted value of (6.60 g/l) predicted by the model. Amino acid analyzer analysis for the produced amino acids shows the release of asparagine, threonine, serine, glutamine, proline, glycine, alanine, cysteine, valine, methionine, isoleucine, leucine, tyrosine, phenyl alanine, histidine, lysine and arginine, respectively. Effect of chicken feather hydrolysate on cucumber powdery mildew disease was tested by applying foliar application with different concentrations (0, 5, 10, 15, and 20% v/v), then degree of infection and sporulation on cucumber plants were assessed. The lowest concentration of chicken feather hydrolysate showed the lowest effect on disease index. Conversely, cucumber resistance increased by the increasing of feather’s hydrolysate concentrations associated with a clear reduction in the disease index and sporulation. Aside from, extra foliar application showed a decrease in the disease index for all concentrations compared with untreated plants. Foliar application with 20% concentration of chicken feather hydrolysate had the highest stimulation of the studied oxidative enzymes i.e., peroxidase (POX), phenylalanine ammonia-lyase (PAL), polyphenol oxidase (PPO) and superoxide dismutase (SOD).

Characterization of methyl-accepting chemotaxis proteins (MCPs) for amino acids in plant-growth-promoting rhizobacterium Pseudomonas protegens CHA0 and enhancement of amino acid chemotaxis by MCP genes overexpression.

cDNA: complementary DNA; LBD: ligand-binding domain; MCP: methyl-accepting chemotaxis protein; PDC: PhoQ/DcuS/CitA; PGPR: plant-growth-promoting rhizobacteria; qRT-PCR: quantitative reverse transcription PCR.

Structural Determinants within the Adenovirus Early Region 1A Protein Spacer Region Necessary for Tumorigenesis.

It has long been established that group A human adenoviruses (HAdV-A12, -A18, and -A31) can cause tumors in newborn rodents, with tumorigenicity related to the presence of a unique spacer region located between conserved regions 2 and 3 within the HAdV-A12 early region 1A (E1A) protein. Group B adenoviruses are weakly oncogenic, whereas most of the remaining human adenoviruses are nononcogenic. In an attempt to understand better the relationship between the structure of the AdE1A spacer region and oncogenicity of HAdVs, the structures of synthetic peptides identical or very similar to the adenovirus 12 E1A spacer region were determined and found to be α-helical using nuclear magnetic resonance (NMR) spectroscopy. This contrasts significantly with some previous suggestions that this region is unstructured. Using available predictive algorithms, the structures of spacer regions from other E1As were also examined, and the extent of the predicted α-helix was found to correlate reasonably well with the tumorigenicity of the respective virus. We suggest that this may represent an as-yet-unknown binding site for a partner protein required for tumorigenesis.IMPORTANCE This research analyzed small peptides equivalent to a region within the human adenovirus early region 1A protein that confers, in part, tumor-inducing properties to various degrees on several viral strains in rats and mice. The oncogenic spacer region is α-helical, which contrasts with previous suggestions that this region is unstructured. The helix is characterized by a stretch of amino acids rich in alanine residues that are organized into a hydrophobic, or "water-hating," surface that is considered to form a major site of interaction with cellular protein targets that mediate tumor formation. The extent of α-helix in E1A from other adenovirus species can be correlated to a limited degree to the tumorigenicity of that virus. Some serotypes show significant differences in predicted structural propensity, suggesting that the amino acid type and physicochemical properties are also of importance.

Inhalation of odors containing DMHF generated by the Maillard reaction affects physiological parameters in rats

The effects of odors generated by the Maillard reaction from amino acids and reducing sugars on physiological parameters (blood pressure, heart rate, and oxidative stress levels) in Wistar rats were investigated in the present study. The Maillard reaction samples were obtained from glycine, arginine, or lysine of 1.0 mol/L and glucose of 1.0 mol/L with heat treatment. The odor-active compounds in the Maillard reaction samples were identified using the aroma extract dilution analysis. Among the odor-active compounds identified, 2,5-dimethyl-4-hydroxy-3(2H)-furanone (DMHF, FURANEOL and strawberry furanone) had the highest odor activity and its concentration was affected by amino acid types. The Maillard reaction odors generated from glycine or arginine significantly decreased systolic blood pressure and heart rate in rats when inhaled. These physiological effects were associated with DMHF. Furthermore, oxidative stress marker levels in rat plasma were decreased by the inhalation of DMHF. The inhalation of DMHF appears to at least partly affect physiological parameters by decreasing oxidative stress.

Conserved internal hydration motifs in protein kinases.

Crystal structures of diverse protein kinase catalytic subunits reveal a number of water molecules whose positions within the protein core are better preserved than amino acid types in many functionally important locations. It remains unknown whether they play any particular role, and whether their removal, disturbing local interaction patterns to no smaller degree than amino acid mutations, can affect kinase stability and function. In this study, we apply an array of computational approaches to characterize hydration of kinase catalytic subunits. First, we systematically screen multiple crystal structures with the use of a simplified hydration model in order to determine the distribution of internal solvent and the degree of its conservation. Second, we analyze water structure, dynamics and binding affinity to buried hydration sites in a number of kinases, also taking into account their variable functional state. We find that a large portion of buried solvent is dynamic, possibly contributing to kinase conformational changes related to the activation process. In turn, binding free energies of some of tightly bound conserved water molecules to different kinases tend to shift in a similar manner following the change of their functional state. This finding highlights the likely specific role of internal solvent in fine tuning local protein plasticity.

Bioactivity evaluation of amino acid-conjugates with protein versus cellulose based conjugates and extracted flavonoids

The work in this article was done to evaluate the performance of new protein-based bioactive compounds for treating the cancer cells. These bioactive compounds were synthesized by condensation reaction of sodium caseinate with amino acids in absence of solvent and evidenced by FTIR, TGA and DSC analyses. The bioactivity of these protein-based conjugates (SC-conjugates), was evaluated towards different cancer cell lines such as Breast MCF7, Colon HCT116, Lung A549 and Human hepatocellular carcinoma HePG2) in comparison with sodium carboxymethyl cellulose-amino acid SCMC-conjugates. Two types of amino acids (phenylalanine and methionine) were used to evaluate the role of phenyl group contained in the amino acid on bioactivity performance. The effective role and safety behavior of the conjugates were assessed from the values of selectivity index against RPE1 [normal retina cell line], moreover their cancer inhibition versus natural extracted flavonoids whether individually or in hybrid.The results showed the effective performance of SC-PA conjugate in inhibiting the cancer cell proliferation, of most examined cancer cell lines, especially against breast cancer MCF7 and colon HCT116 (IC50 and IC90 are 39.8–44.1 μg/mL and 71.7–83.6 μg/mL, respectively). IC50 of this conjugate for MCF7 was equivalent to Rutin natural flavonoid. The Rutin has synergistic inhibition effect to MCF7 when it used in hybrid with SC-PA, at which it leads to decrease the IC50 from 39.8 to 33.1 μg/mL.

Transformation of nitrogen during hydrothermal carbonization of sewage sludge: Effects of temperature and Na/Ca acetates addition

This study reports the effects of temperature and Ca/Na acetates addition on the transformation of nitrogen during hydrothermal carbonization of sewage sludge at 160–250 °C. The nitrogen species in the hydrochar, aqueous, oil and gas products from sludge hydrothermal carbonization at different temperatures are well characterized, with a focus on the amino acid species in various products. Temperature is found to greatly affect the nitrogen transformation during sludge hydrothermal carbonization. At 160 °C, 47.3% of nitrogen is transformed into the aqueous product. When the temperature increases to 250 °C, only 27.1% of nitrogen is retained in the hydrochar, while 69.2 and 6.7% of nitrogen is present in the aqueous and oil products, respectively. During hydrothermal carbonization, the protein-N is first converted into the polypeptide-N in the aqueous product, followed by its further decomposition into the NH+ 4-N. This leads to a high content of the NH+ 4-N in the aqueous product, especially at increased temperatures. The labile protein-N is also transformed into the heterocylic-N (especially the pyrrole-N) in the hydrochar as the temperature increases. Among all nitrogen species in the aqueous product, the polypeptide-N consisting of amino acids with the alkyl group is the most stable. Moreover, the addition of NaAc and CaAc2 reduces the nitrogen retention in the hydrochar, mainly due to enhanced hydrolysis of the protein-N. While for CaAc2 addition, the deamination of the polypeptide-N is also enhanced, leading to a higher NH+ 4-N in the aqueous product. Our results show that the type of amino acid in protein is important to determine the nitrogen transformation pathways, and acetate addition is an important strategy for enhancing nitrogen removal in the hydrochar during hydrothermal carbonization.

Corrosion Behavior and In Vitro Cytotoxicity of Ni-Ti and Stainless Steel Arch Wires Exposed to Lysozyme, Ovalbumin, and Bovine Serum Albumin.

In this study, the tendency and mechanisms by which protein and mechanical loads contribute to corrosion were determined by exposing Ni–Ti and stainless steel arch wires under varying mechanical loads to artificial saliva containing different types of protein (lysozyme, ovalbumin, and bovine serum albumin). The corrosion behavior and in vitro cytotoxicity results show that exposure to both protein and mechanical stress significantly decreased the corrosion resistance of stainless steel and increased the release of toxic corrosion products. Adding protein inhibited the corrosion of Ni–Ti, but the mechanical loads counteracted this effect. Even proteins containing the same types of amino acids had different effects on the corrosion resistance of the same alloy. The effect of protein or stress, or their combination, should be considered in the application of metal medical materials.

Measurement and visualization of cell membrane surface charge in fixed cultured cells related with cell morphology.

The diagnosis of patients with malignancies relies on the results of a clinical cytological examination. To enhance the diagnostic qualities of cytological examinations, it is important to have a detailed analysis of the cell’s characteristics. There is, therefore, a need for developing a new auxiliary method for cytological diagnosis. In this study, we focused on studying the charge of the cell membrane surface of fixed cells, which is one of important cell’s characteristics. Although fixed cells lose membrane potential which is observed in living cells owing to ion dynamics, we hypothesized that fixed cells still have a cell membrane surface charge due to cell membrane components and structure. We used 5 cell lines in this study (ARO, C32TG, RT4, TK, UM-UC-14). After fixation with CytoRich Red, we measured the cell membrane surface charge of fixed cells in solution using zeta potential measurements and fixed cells on glass slides, visualizing it using antibody-labeled beads and positively-charged beads. Furthermore, we measured the cell membrane surface charge of fixed cells under different conditions, such as different solution of fixative, ion concentration, pH, and pepsin treatments. The zeta potential measurements and visualization using the beads indicated that the cell membrane surface of fixed cells was negatively charged, and also that the charge varied among fixed cells. The charge state was affected by the different treatments. Moreover, the number of cell-bound beads was small in interphase, anaphase, and apoptotic cells. We concluded that the negative cell membrane surface charge was influenced by the three-dimensional structure of proteins as well as the different types of amino acids and lipids on the cell membrane. Thus, cell surface charge visualization can be applied as a new auxiliary method for clinical cytological diagnosis. This is the first systematic report of the cell membrane surface charge of fixed cells.

ANALISIS PROTEIN DAN ASAM AMINO NATTO, MAKANAN FERMENTASI KEDELAI KUNING OLEH BASILLUS SUBTILLIS NATTO

This Research aims to analyze crude protein and amino acid profile of natto from yellow soybeans from Vedca Cianjur. Protein analysis was performed using the Semi-micro Kjeldahl method, while amino acid analysis was performed using High Performance Liquid Chromatography (HPLC). Analysis of natto paste shows that natto contains an average of 22.1% crude protein and an average amino acid content of 14.46%. The results of the analysis of 15 average amino acids in Natto with HPLC showed that amino acids consist of 7 types of essential amino acids and 8 essential amino acids. The percentage of fresh weight of essential amino acids are Histidine (0.46% wb), Leucine (1.25% wb), Threonine (0.59%wb), Valine (0.81% wb), Methionine (0.13% wb), Isoleucine (0,76% wb), Fenilalanine (0.87% wb) and 8 non-essential amino acids are Serine (0.72% wb), Aspartic Acid (1.89%), Arginine (0.91%), Lysine (0.83% ), Glutamine (3.62%), Glycine (0.65%), Alanin (0.67%), and Tyrosine (0.3% wb). Glutamine is the highest level of amino acids (3.62% wb), followed by aspartic acid (1.89% wb) and Leucine (1.25% wb).