Newsletter 05/2024 edited by Loredano Pollegioni

PollegioniThe 6th International Conference of D-Amino Acid Research (IDAR2024) and 18th JointConference of the D-Amino Acid Research Society Japan was successfully held at KanazawaUniversity on August 21-24 2024

The 6th International Conference of D-Amino Acid Research (IDAR2024) and 18th Joint Conference of the D-Amino Acid Research Society Japan was successfully held at Kanazawa University on August 21-24 2024

See all of you in France in 2026!!

Do you have news concerning the D-amino acids field to announce? Is there a relevant published paper to mention? Write us and take the advantage of this bimonthly Newsletter.

The Editor’s pick selection of the most intriguing papers is highlighted in yellow.

05/2024

D-AAs AND PATHOLOGIES:

Decreased free D-aspartate levels in the blood serum of patients with schizophrenia

Garofalo M, De Simone G, Motta Z, Nuzzo T, De Grandis E, Bruno C, Boeri S, Riccio MP, Pastore L, Bravaccio C, Iasevoli F, Salvatore F, Pollegioni L, Errico F, de Bartolomeis A, Usiello A
Front Psychiatry. 2024 Jul 10;15:1408175. doi: 10.3389/fpsyt.2024.1408175.
Schizophrenia (SCZ) and autism spectrum disorder (ASD) are neurodevelopmental diseases characterized by different psychopathological manifestations and divergent clinical trajectories. This paper reports about a bicentric study to assess the blood serum levels of NMDA receptors-related glutamatergic amino acids and their precursors, including L-glutamate, L-glutamine, D-aspartate, L-aspartate, L-asparagine, D-serine, L-serine and glycine, in ASD, SCZ patients and control subjects. The SCZ patients were subdivided into treatment-resistant and non-treatment-resistant patients, based on their responsivity to conventional antipsychotics. D-serine and D-aspartate serum reductions were found in SCZ patients compared to controls while no significant differences between cases and controls were evident in amino acid concentrations in the two ASD cohorts.

Exploration of the intracellular chiral metabolome in pediatric BCP-ALL: a pilot study investigating the metabolic phenotype of IgH locus aberrations
Collins M, Gorgoglione R, Impedovo V, Pan X, Chakkarai S, Yi SS, Lodi A, Tiziani S
Front Oncol. 2024 Aug 5;14:1413264. doi: 10.3389/fonc.2024.1413264.
Aberrations in the immunoglobulin heavy chain (IgH) locus are associated with poor prognosis in pediatric precursor B-cell acute lymphoblastic leukemia (BCP-ALL) patients. Here, leukemia cells were isolated from the bone marrow of BCP-ALL pediatric patients at diagnosis and metabolome and transcriptome were characterized. For the first time, D-amino acids were identified in the leukemic cells’ intracellular metabolome from the bone marrow niche. Chiral metabolic signatures at diagnosis was indicative of a resistant phenotype. Through integrated network analysis and Pearson correlation, confirmation was obtained regarding the association of the IgH phenotype with several genes linked to poor prognosis.

Specific inhibitory effects of exogenous D-aspartate on the proliferation of intestinal epithelial cells
Takizawa Y., Furuya T., Uno M., Ohashi R., Mimura E., Kurita T., Nakajima T.
Biochemical and Biophysical Research Communications (2024) 734, art. no. 150659, doi: 10.1016/j.bbrc.2024.150659
This work examined the effects of D-amino acids on gastrointestinal tract basal cells. The effects of 11 amino acids (Ala, Arg, Asn, Asp, Gln, Glu, Leu, Lys, Pro, Ser, and Val) on the proliferation of three types of gastrointestinal epithelial cells (HGC-27, IEC-6, and Caco-2) were assessed. Although the proliferation of HGC-27 and Caco-2 cells was not affected by any of the 11 types of L- and D-AAs. D-Asp inhibited the proliferation of IEC-6, derived from small intestinal epithelial cells, in concentration- and exposure time-dependent manners. The uptake transporters, metabolic enzymes, and insulin signaling pathways were also investigated, but the mechanisms related to the inhibitory effects of D-Asp on the proliferation of IEC-6 were not elucidated.

D-Glutamate production by stressed Escherichia coli gives a clue for the
hypothetical induction mechanism of the ALS disease
Monselise E.B.-I., Vyazmensky M., Scherf T., Batushansky A., Fishov I.
Scientific Reports (2024) 14 (1), art. no. 18247, doi: 10.1038/s41598-024-68645-8.
In the search for the origin of Amyotrophic Lateral Sclerosis disease (ALS), the authors previously proposed that D-amino acids produced by stressed microbiome may serve as inducers of the disease development. Here, wild-type Escherichia coli cells were subjected to carbon and nitrogen starvation stress: D-glutamate accumulated in the stressed bacteria but not in control cells. D-Glu produced by the stressed microbiome, could induce neurobiochemical miscommunication setting on C1q of the complement system, this suggesting preventive medicine approaches to ALS, Alzheimer, and Parkinson.

Urinary D-asparagine level is decreased by the presence of glioblastomas

INakade Y., Kinoshita M., Nakada M., Sabit H., Ichinose T., Mita M., Yuno T., Noguchi-Shinohara M., Ono K., Iwata Y., Wada T.
Acta Neuropathologica Communications (2024) 12 (1), art. no. 122, doi: 10.1186/s40478-024-01836-6.
This study aimed to identify novel biomarkers for gliomas, particularly glioblastomas (GBMs), using chiral amino acid profiling on resected tissues (tumor and non-tumor), blood, and urine from 33 patients with primary gliomas and 24 healthy volunteers. D-asparagine (D-Asn) levels were higher and D-amino acid oxidase (DAAO) expression was lower in glioma than in non-glioma tissues. Blood and urinary D-Asn levels were lower in patients with GBM than in healthy volunteers, increasing after GBM removal. Urinary D-Asn levels differentiated between healthy volunteers and patients with GBM. GBM mouse model validated the decrease of urinary D-Asn in GBM. GBM cells used D-Asn for cell proliferation. Gliomas induce alterations in chiral amino acid profiles, affecting blood and urine levels. Urinary D-Asn emerges as a promising diagnostic biomarker for gliomas, reflecting tumor presence and severity.

LC-MS analysis of chiral amino acids in human urine reveals D-amino acids as
potential biomarkers for colorectal cancer

IDeng W., Ye C., Wang W., Huang R., Guo C., Pan Y., Sun C.
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences (2024) 1245, art. no. 124270, doi: 10.1016/j.jchromb.2024.124270.
Colorectal cancer (CRC) is a common malignant tumor in the gastrointestinal tract. In this study the quantification of L- and D-amino acids in urine samples collected from 115 CRC patients and 155 healthy volunteers was reported. The method of chiral labeling, liquid chromatography, and tandem mass spectrometry enabled separation and detection of 28 amino acids (14 L-amino acids, 13 D-amino acids and Gly). Orthogonal partial least squares discriminant analysis identified 14 targeted variables among these chiral amino acids that
distinguished the CRC from the healthy controls. Binary logistic regression analysis revealed that D-α-aminobutyric acid, L-alanine, D-alanine, D-glutamine and D-serine could be potential biomarkers for CRC. D-Ala, D-Gln, and D-Ser achieved an AUC of 0.988, indicating important contributions of D-amino acids to the association with CRC. Furthermore, the metabolic aberration was associated with age and the development of CRC: D-methionine was decreased in CRC patients with age over 50, and D/L-Gln in patients at stage IV was higher than patients at stage I.

D-AAS & PHYSIOLOGICAL ROLES:

New insights into D-aspartate signaling in testicular activity
Falvo S., Santillo A., Di Fiore M.M., Venditti M., Grillo G., Latino D., Baccari I., Petito G., Chieffi Baccari G.
Cells (2024) 13 (16), art. no. 1400, doi: 10.3390/cells13161400.
This review focuses on D-aspartate (D-Asp), which is found in high concentrations in the testis and pituitary gland, highlighting D-amino acids as promising candidates in promoting spermatogenesis. Increasing evidence suggests that D-Asp promotes spermatogenesis by activating testosterone production in the Leydig cells via LH release from the pituitary gland. In vitro studies indicate that D-Asp may also influence steroidogenesis and spermatogenesis through autocrine and paracrine signals. D-Asp enhances StAR and steroidogenic enzyme expressions, facilitating testicular cell proliferation via the GluR/ERK1/2 pathway. Moreover, it supports spermatogenesis by enhancing the mitochondrial function in spermatocytes, aiding in the metabolic shift during meiosis. D-Asp also exerts a notable anti-apoptotic effect in the testis via the AMPAR/AKT pathway, potentially mediated by antioxidant enzyme modulation to mitigate testicular oxidative stress.

D-AAS & BIOTECHNOLOGY:

Effect of novel and traditional intracanal medicaments on biofilm viability and composition
Siu SY, Pudipeddi A, Vishwanath V, Cheng Lee AH, Tin Cheung AW, Pan Cheung GS, Neelakantan P
J Endod. 2024 Jul 15:S0099-2399(24)00398-4. doi: 10.1016/j.joen.2024.07.003.
This study evaluated the hypothesis that a combination of D-amino acids (D-AAs) and trans-cinnamaldehyde (TC) should possess superior antibiofilm activity to calcium hydroxide (CH) and untreated controls. At first, the concentration of D-methionine, D-leucine, D-tyrosine, and D-tryptophan that would significantly decrease Enterococcus faecalis and Actinomyces naeslundii biofilm biomass was determined. Then, 0.06% TC, 1 mM D-tyrosine and 25 mM D-tryptophan significantly reduced the biomass and biofilm viability compared to the control. While no significant difference was observed between TC+D-AAs and CH in the cultivable bacterial counts, a significantly greater percentage of dead bacteria was apparent in TC + D-AAs-treated biofilms compared to CH and the control. TC+D-AAs significantly decreased the biovolume and all the examined components of the biofilm matrix compared to the control, while CH significantly reduced only the exopolysaccharide quantity.

Metabolic labeling of peptidoglycan enabled optical analysis of probiotic vitality
Hu X, Xiong Q, Hou S, Duan H
Anal Methods. 2024 Aug 27. doi: 10.1039/d4ay00982g. Online ahead of print To develop probiotic functional foods that deliver health benefits, it is essential to characterize both probiotic viability and vitality. Here, a D-amino-acid-based metabolic labeling strategy was applied to quantitatively depict probiotic vitality: probiotics were first metabolically incorporated with azido-modified D-lysine and then labeled with dibenzocyclooctyne-sulfo-Cy5 through click chemistry. This two-step labeling process provides a visual representation of the metabolic levels of probiotics as well as the bacterial membrane integrity. This rapid detection process has the potential to be widely implemented in the food industry for probiotic vitality evaluation.

Transient infection of Euprymna scolopes with an engineered D-alanine auxotroph of Vibrio fischeri
Coppinger M, Yang L, Popham DL, Ruby E, Stabb EV
Appl Environ Microbiol. 2024 Sep 5:e0129824, doi: 10.1128/aem.01298-24. Online ahead of print
TThe symbiosis between Vibrio fischeri and the Hawaiian bobtail squid, Euprymna scolopes, is a tractable and well-studied model of bacteria-animal mutualism. Here, a method to transiently colonize E. scolopes using D-alanine (D-ala) auxotrophy of the symbiont, controlling the persistence of viable infection by supplying or withholding D-ala, was reported. The authors generated alanine racemase (alr) mutants of V. fischeri that lack avenues for mutational suppression of auxotrophy or reversion to prototrophy. This study highlights a new approach for inducing transient colonization and provides insight into the biogeography of the E. scolopes light organ.

Interfacially crystallized Enzyme@MOFs biocatalytic membranes for highly efficient synthesis of D-amino acids via continuously recirculating stereoinversion
Liu G., Wang L., Gao Z., Feng C., Liu Q., Chen X.
Chemical Engineering Journal (2024) 497, art. no. 154529, doi: 10.1016/j.cej.2024.154529.
This study focused on the coating of polyvinylidene fluoride (PVDF) hollow fiber membrane with L-amino acid oxidase (LAAO) embedded zeolitic imidazolate framework-8 (ZIF-8) layer by a single-step interfacial biomineralization strategy for efficient synthesis of D-amino acids. This biocatalytic membrane only oxidizes the L-AAs, and the D-AAs accumulated after multiple rounds of continuously recirculating stereoinversion. When tryptophan was used, a 92.1% conversion rate and a 99.4% ee of D-Trp was generated.

Highly efficient chiral extraction of amino acid enantiomers using Wei-Phos-Pd as chiral extractant
Liu X., Qin S., Yang Y., Qiu S., Tang X., Peng L., Li S.
Separation and Purification Technology (2025) 354, art. no. 129187, doi: 10.1016/j.seppur.2024.129187.
In this work, Wei-Phos, an adaptive chiral sulfinamide phosphine ligand featuring multiple coordination centers, was employed as a chiral extractant to separate amino acid enantiomers: D-AAs are preferentially recognized by Wei-Phos-Pd. The separation factors for phenylalanine (Phe), homophenylalanine (Hph), 3-chlorophenylglycine (3-Cl-Phg), and 4-nitro-phenylalanine (4-NO2-Phe) are 12.2, 8.9, 13.2 and 7.1, respectively.

Biological evaluation of D-[18F]Fluoroalanine and D-[18F]Fluoroalanine-d3 as positron emission tomography imaging tracers for bacterial infection
Li K., Tolentino Collado J., Marden J.A., Pollard A.C., Guo S., Tonge P.J., Qu W.
Journal of Medicinal Chemistry (2024) 67 (16): 13975-13984, doi: 10.1021/acs.jmedchem.4c00783.
TD-Fluoroalanine and the deuterium-labeled analogue fludalanine (MK641) were originally explored as antibiotics by Merck but failed in clinical trials due to unaccepted toxicity. Herein, a fluorine-18 labeled D-fluoroalanine, D-3-[18F]fluoroalanine (D-[18F]FAla), and its deuterated analogue, D-3-[18F]fluoroalanine-d3 (D-[18F]FAla-d3) were produced and evaluated. Both peptides accumulated up to 0.64-0.78% ID/cc in the infectious area at 15 min post-injection. These radiolabeled D-alanine analogues were able to differentiate bacterial infection from sterile inflammation in a soft-tissue model of S. aureus infection.

ENZYMES ACTIVE ON D-AAS:

Hierarchical engineering of meso-diaminopimelate dehydrogenase for efficient synthesis of bulky D-amino acids
Wei Y., Geng Q., Liu H.-P., Wang Y.-Q., Zhang G.-F., Qian X.-L., Yu H.-L., Xu J.-H., Zhang Z.-J. ACS Catalysis (2024) 14 (15), pp. 11447 – 11456, doi: 10.1021/acscatal.4c03164.
Asymmetric reductive amination of α-ketoacids by D-amino acid dehydrogenase is a straightforward and promising method for the synthesis of D-amino acids: the engineered meso-diaminopimelate dehydrogenases (DAPDHs) can be applied on this side. Anyway, DAPDH variants showed restricted activity toward bulky α-ketoacids: here, the activity of a DAPDH from Bacillus thermozeamaize toward a number of α-ketoacids was improved by engineering of the active pocket. The best variant M5 exhibits a specific activity of up to 1.65 U mg-1 toward bulky benzoylformic acid, which is 275-fold that of the wild type, with no reduction in thermostability. Using M5 as a biocatalyst, three pharmaceutically relevant compounds, D-phenylglycine, D-phenylalanine, and D-homophenylalanine, were prepared on a gram scale in up to 89% yield and >99% ee.

Multifunctionality of a low-specificity L-threonine aldolase from the hyperthermophile Thermotoga maritima
Miyamoto T., Kobayashi F., Emori K., Sakai-Kato K.
Extremophiles (2024) 28 (3), art. no. 41, doi: 10.1007/s00792-024-01357-z.
The peptidoglycan of the hyperthermophile Thermotoga maritima contains an unusual D-lysine in addition to the typical D-alanine and D-glutamate. Here, the enzymatic properties of threonine aldolase TM1744 were studied to probe both its potential multifunctionality and D-amino acid metabolizing activities. TM1744 displayed aldolase activity toward both L-allo-threonine and L-threonine, and exhibited higher activity toward L-threo-phenylserine. It did not function as an aldolase toward D-allo-threonine or D-threonine. Furthermore, TM1744 had racemase activity toward two amino acids, although its racemase activity was lower than aldolase one. Notably, TM1744 did not have other amino acid metabolizing activities.

Improving the enzymatic activity and stability of N-carbamoyl hydrolase using deep learning approach
Zhang F., Naeem M., Yu B., Liu F., Ju J.
Microbial Cell Factories (2024) 23 (1), art. no. 164, doi: 10.1186/s12934-024-02439-5.
The two-enzyme cascade reaction based on the enzymes DHdt and DCase represents an efficient way to produce D-amino acids, but DCase is susceptible to heat inactivation. Here, the rational design software “Feitian” was developed based on kcat prediction using the deep learning approach. Six single-point variants with high kcat value were selected: three variants (Q4C, T212S, and A302C) showed higher enzymatic activity than the wild-type. Furthermore, the combined triple-point mutant DCase-M3 (Q4C/T212S/A302C) exhibited a 4.25-fold increase in activity and a 2.25-fold increase in thermal stability as compared to the wild-type. The whole-cell reaction allowed to reach a high titer of D-HPG (2.6 mM) by using the Q4C/T212S/A302C variant.

D-AAS IN MICROORGANISMS:

Bioinformatic approaches identify hybrid antibiotics against tuberculosis via D-
amino acid-activating adenylation domains from Cordyceps militaris
Gao Y, Liao L, Xu Y, Huang J, Gao J, Li L
J Nat Prod. 2024 Aug 23;87(8):2110-2119. doi: 10.1021/acs.jnatprod.4c00718.
Tuberculosis represents a global challenge, with the emergence of multidrug-resistant Mycobacterium tuberculosis. Here, a bioinformatic approach was employed to investigate D-amino acid-activating adenylation domains, leading to the identification of cordysetin A (1), a novel trans-decalin tetramic acid
antibiotic from the ascomycete fungi Cordyceps militaris. Cordysetin A (1) exhibits considerable activity against M. tuberculosis in vitro and in vivo while maintaining low cytotoxicity.

D-aspartate, an amino-acid important for human health, supports anaerobic
respiration in several Campylobacter species

Benoit S.L., Maier R.J.
Research in Microbiology (2024) 175 (7), art. no. 104219, doi: 10.1016/j.resmic.2024.104219.
Most Campylobacter species can grow anaerobically using formate or molecular hydrogen as electron donors, and various nitrogenous and sulfurous compounds as electron acceptors. This work demonstrates that both L-asparagine and L-aspartic acid bolster H2-driven anaerobic growth in several Campylobacter species, whereas D-Asn and D-Asp only increased anaerobic growth in Campylobacter concisus strain 13826 and Campylobacter ureolyticus strain NCTC10941. A gene annotated as racD encoding for a putative Asp racemase was identified in both strains: this work suggests that the racD gene is required for campylobacters to use either D-Asp or D-Asn. The ability to use D-Asp by various human opportunistic bacterial pathogens (C. concisus, C. ureolyticus, and select strains of Campylobacter gracilis, Campylobacter rectus and Campylobacter showae) is of main relevance since D-Asp is an important signal molecule for both human nervous and neuroendocrine systems.

D-AAS IN PEPTIDES AND PROTEINS:

D-Peptide cell culture scaffolds with enhanced antibacterial and controllable release properties
Tian Y, Hou Y, Tian J, Zheng J, Xiao Z, Hu J, Zhang Y
J Mater Chem B. 2024 Aug 22;12(33):8122-8132. doi: 10.1039/d4tb00969j.
In this study, a peptide (termed D-IK1) entirely consisting of D-amino acids was produced: it is an enantiomer of a previously reported AMP IK1. This peptide showed remarkably improved antibacterial and anticancer activities, and self-assembled into hydrogels that effectively inhibited bacterial and cancer cell growth by the controlled and sustained release of D-IK1. D-IK1 was also extremely stable in salt solutions and resisted serum and protease degradation. D-IK1 hydrogel fostered cell adhesion and proliferation, proving its viability as a 3D scaffold for cell culture applications. It shows the potential for applications in cell culture, wound healing, and the eradication of multidrug-resistant bacterial infections.

Mirror-image random nonstandard peptide integrated discovery (MI-RaPID) technology yields highly stable and selective macrocyclic peptide inhibitors for matrix metallopeptidase 7
Metanis N, Ghareeb H, Li CY, Shenoy A, Rotenberg N, Shifman JM, Katoh T, Sagi I, Suga H Angew Chem Int Ed Engl. 2024 Aug 30:e202414256, doi: 10.1002/anie.202414256.
Matrix metallopeptidase 7 (MMP7) plays a crucial role in cancer metastasis and progression, making it an attractive target for therapeutic development. Here, mirror-image random nonstandard peptides integrated discovery (MI-RaPID) technology was used to discover innate protease-resistant macrocyclic peptides that specifically bind to and inhibit human MMP7. The macrocyclic peptide D20 was synthesized in its mirror-image form, D’20, consisting of 12 D-amino acids, one cyclic β-amino acid, and a thioether bond. It inhibited MMP7 with an IC50 value of 90 nM, and showed excellent selectivity over other MMPs with similar substrate specificity. Moreover, D’20 inhibited the migration of pancreatic cell line CFPAC-1, but had no effect on the cell proliferation and viability. D’20 exhibited excellent stability in human serum, as well as in simulated gastric and intestinal fluids.

The immunosuppressive properties of cyclo-[D-Pro-Pro-β(3)-HoPhe-
Phe-]tetrapeptide selected from stereochemical variants of cyclo-[Pro-Pro-β(3)-HoPhe-Phe-] peptide
Kaczmarek K, Artym J, Bojarska J, Pacholczyk-Sienicka B, Waśko J, Jelemenska I, Wolf WM, Breza M, Zimecki M
Pharmaceutics. 2024 Aug 22;16(8):1106, doi: 10.3390/pharmaceutics16081106.
The anti-inflammatory, antiviral, and anti-cancer properties, as well as the mechanism of action of cyclo-[Pro-Pro-β3-HoPhe-Phe-] tetrapeptide (called 4B8M) were recently described. Here, the immunosuppressive actions of the stereochemical variants of 4B8M obtained by sequential substitution of L-amino acids by D-amino acids was studied. All peptides were non-toxic to human peripheral blood mononuclear cells (PBMCs) and only cyclo-[D-Pro-Pro-β3-HoPhe-Phe-] peptide (P03) was capable of inhibiting mitogen-induced PBMC proliferation. The peptides inhibited the LPS-induced production of tumor necrosis factor-alpha to various degrees. P03 demonstrated comparable, or even better, anti-inflammatory and bio-pharmacokinetic properties to 4B8M and may be considered as a potential therapeutic.

D-AAS AND ANALYTICAL METHODS:

Simultaneous analysis of DL-amino acids in foods and beverages using a highly sensitive chiral resolution labeling reagent
Ozaki M., Nakade T., Shimotsuma M., Ikeda A., Kuranaga T., Kakeya H., Hirose T.
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences (2024) 1244, 124239, doi: 10.1016/j.jchromb.2024.124239.
In this work a simple method for the rapid separation and highly sensitive detection of D,L-amino acids in various foods and beverages by liquid chromatography–mass spectrometry (LC–MS) using an octadecyl (C18) column after labeling with 1-fluoro-2,4-dinitrophenyl-5-D-leucine-N,N-dimethylethylenediamineamide (D-FDLDA; e. e. > 99.9 %) is reported. Furthermore, using a stable isotope (13C6)-labeled D-FDLDA (13C6-D-FDLDA) an analytical method that can accurately identify the peak of each D,L-amino acid was established. MS sensitivity of D,L-amino acids labeled with this labeling reagent was higher than that of conventional labeling reagents (Marfey’s reagents).

D-AAS AND FOOD:

Assaying D-amino acid in Japanese sake using L-amino acid derivatizing agent

Kato H, Kanauchi M
Methods Mol Biol. 2024;2851:125-131, doi: 10.1007/978-1-0716-4096-8_11.
TD-Alanine, D-glutamic acid, and D-aspartic acid are known to increase tasting evaluation scores of Sake. Kimoto is brewed using lactic acid bacteria growth to decrease pH. Sake brewed using the Kimoto method also has a rich taste and a higher tasting evaluation score than Sake brewed using the Sokujyo Syubo (Moto) method, which adds lactic acid instead of using lactic acid bacteria growth. D-alanine, D-glutamic acid, and D-aspartic acid in Sake have the function of increasing tasting evaluation scores. They are converted by enzymes in lactic acid bacteria in Kimoto Mash.

INFORMATION

The D-amino acids International Research Center “DAAIR“ has been established in Gerenzano (Varese, Italy) in 2019 with the aim to support and perform scientific research projects and activities on the field of D-amino acids. The Center, located inside the Fondazione Istituto Insubrico Ricerca per la Vita, is aimed to represent a pole of excellence at international level for dissemination and research involving the D-amino acids (Director Silvia Sacchi).

Info@d-aminoacids.com

director@d-aminoacids.com

D-AMINO ACIDS INTERNATIONAL RESEARCH CENTER

INFO@D-AMINOACIDS.COM