SEARCH · Engineering Papers

Results for “polyamine”

Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 37 records · Page 2

All sources NASA NTRS DOE OSTI

DOE OSTI2025

N-terminal domain swapping: A new paradigm for spermidine/spermine N -acetyltransferase (SSAT) protein structures?

Enterococcus faecalis is a multi-drug-resistant human pathogen that is found in a variety of environments and is challenging to treat. Under stress conditions, some bacteria regulate intracellular polyamine concentrations via polyamine acetyltransferases to reduce their toxicity. The E. faecalis genome encodes two polyamine acetyltransferases: PmvE and BltD. Both of these proteins belong to the Gcn5-related N-acetyltransferase (GNAT) superfamily. It is unclear why there are two enzymes with similar substrate specificities in this organism. To better understand the structure/function relationship of the E. faecalis BltD enzyme, we determined its crystal structure and performed additional assays to explore its oligomeric state and enzymatic activity. The goal was to determine whether there were structural or catalytic differences between this enzyme and other polyamine acetyltransferases that could explain this redundancy and be exploited for future development of targeted inhibitors for this important human pathogen. We found the BltD enzyme was structurally unique due to its N-terminal domain swapped dimer. However, this enzyme adopts a catalytically active monomer rather than dimer in solution. This indicates the crystal structure we obtained may represent a state that forms at high protein and salt concentrations and at low pH used during crystallization. The BltD dimer found in the crystal may represent a unique view of how an inhibitory peptide or molecule could be designed to occupy its active site. Additionally, this structure shows the extensive flexibility of the N-terminal portion of the E. faecalis BltD enzyme.

59 BASIC BIOLOGICAL SCIENCES↗

DOE OSTI2022

Probing the Kinetic Origin of Varying Oxidative Stability of Ethyl- vs. Propyl-spaced Amines for Direct Air Capture

Amine-based adsorbents are promising for direct air capture of CO 2 , yet oxidative degradation remains a key unmitigated risk hindering wide-scale deployment. Borrowing wisdom from the basic auto-oxidation scheme, insights are gained into the underlying degradation mechanisms of polyamines by quantum chemical, advanced sampling simulations, adsorbent synthesis, and accelerated degradation experiments. The reaction kinetics of polyamines are contrasted with that of typical aliphatic polymers and they elucidate for the first time the critical role of aminoalkyl hydroperoxide decomposition in the oxidative degradation of amino-oligomers. The experimentally observed variation in oxidative stability of polyamines with different backbone structures is explained by the relationship between the local chemical structure and the free energy barrier of aminoalkyl hydroperoxide decomposition, suggesting that its energetics can be used as a descriptor to screen and design new polyamines with improved stability. In conclusion, the developed computational capability sheds light on radical-induced degradation chemistry of other organic functional materials.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2025

Structural, functional, and regulatory evaluation of a cysteine post-translationally modified Gcn5-related N -acetyltransferase

Polyamines within the cell are tightly regulated by spermidine/spermine N-acetyltransferase (SSAT) enzymes. While several SSATs have been investigated in different bacterial species, there is still a significant gap in knowledge about which proteins are functional SSATs in many organisms. For example, while it is known that Pseudomonas aeruginosa synthesizes the polyamine spermidine, the SSAT that acetylates this molecule and its importance in regulating intracellular polyamines remains unknown. We previously identified a candidate Gcn5-related N-acetyltransferase (GNAT) protein from P. aeruginosa (PA2271) that could fulfill this role since it acetylates spermidine, but no further studies were conducted. Here, we explored the structure/function relationship of the PA2271 protein by determining its X-ray crystal structure and performing enzyme kinetics assays. We also identified active site residues that are essential for catalysis and substrate binding. As the study progressed, we encountered results that led us to explore the importance of four cysteine residues on enzyme activity and disulfide bond formation or modification of cysteine residues. We found these cysteine residues in PA2271 are important for protein solubility and activity, and there is an interrelationship between cysteine residues that contribute to these effects. Furthermore, we also found disulfide bonds could form between C 121 and C 165 and speculate that these residues may contribute to redox regulation of PA2271 protein activity.

59 BASIC BIOLOGICAL SCIENCES↗

DOE OSTI2022

A scalable solid-state nanoporous network with atomic-level interaction design for carbon dioxide capture

Carbon capture and sequestration reduces carbon dioxide emissions and is critical in accomplishing carbon neutrality targets. Here, we demonstrate new sustainable, solid-state, polyamine-appended, cyanuric acid–stabilized melamine nanoporous networks (MNNs) via dynamic combinatorial chemistry (DCC) at the kilogram scale toward effective and high-capacity carbon dioxide capture. Polyamine-appended MNNs reaction mechanisms with carbon dioxide were elucidated with double-level DCC where two-dimensional heteronuclear chemical shift correlation nuclear magnetic resonance spectroscopy was performed to demonstrate the interatomic interactions. We distinguished ammonium carbamate pairs and a mix of ammonium carbamate and carbamic acid during carbon dioxide chemisorption. The coordination of polyamine and cyanuric acid modification endows MNNs with high adsorption capacity (1.82 millimoles per gram at 1 bar), fast adsorption time (less than 1 minute), low price, and extraordinary stability to cycling by flue gas. This work creates a general industrialization method toward carbon dioxide capture via DCC atomic-level design strategies.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2020

The Neighboring Subunit Is Engaged to Stabilize the Substrate in the Active Site of Plant Arginases

Arginine acts as a precursor of polyamines in plants in two known pathways, agmatine and ornithine routes. It is decarboxylated to agmatine by arginine decarboxylase, and then transformed to putrescine by the consecutive action of agmatine iminohydrolase and N-carbamoylputrescine amidohydrolase. Alternatively, it can be hydrolyzed to ornithine by arginase and then decarboxylated by ornithine decarboxylase to putrescine. Some plants lack a functional ornithine pathway, but all have one or two arginases that can have dual cellular localization, in mitochondria and plastids. It was recently shown that arginases from Arabidopsis thaliana and soybean act also as agmatinases, thus they can produce putrescine directly from agmatine. Therefore, arginase (together with arginine decarboxylase) can complement putrescine production in plastids, providing a third polyamine biosynthesis pathway in plants. Phylogenetic analysis suggests that arginases, highly conserved in the plant kingdom, create the only group of enzymes recognized in the family of ureohydrolases in plants. Arginases are metalloenzymes with binuclear manganese cluster in the active site. In this work, two arginases from A. thaliana and Medicago truncatula are structurally characterized and their binding properties are discussed. Crystal structures with bound ornithine show that plant hexameric arginases engage a long loop from the neighboring subunit to stabilize α-amino and carboxyl groups of the ligand. This unique ligand binding mode is unobserved in arginases from other domains of life. Structural analysis shows that substrate binding by residues from two neighboring subunits might also characterize some prokaryotic agmatinases. This feature of plant arginases is most likely the determinant of their ability to recognize not only arginine but also agmatine as their substrates, thus, to act as arginase and agmatinase.

59 BASIC BIOLOGICAL SCIENCES↗

DOE OSTI2020

Regenerative adsorbents of modified amines on solid supports

The invention relates to regenerative, solid sorbents for adsorbing carbon dioxide from a gas mixture, including air, with the sorbent including a modified polyamine and a solid support. The modified polyamine is the reaction product of an amine and an epoxide. The sorbent provides structural integrity, as well as high selectivity and increased capacity for efficiently capturing carbon dioxide from gas mixtures, including the air. The sorbent is regenerative, and can be used through multiple cycles of adsorption-desorption.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2021

Regenerative adsorbents of modified amines on solid supports

Goeppert, Alain↗

DOE OSTI2025

Design, Synthesis, and Biological Activity of Novel Ornithine Decarboxylase (ODC) Inhibitors

We here describe the design, synthesis, and biological activity of novel ornithine decarboxylase (ODC) inhibitors that show significantly higher potency in vitro than α-difluoromethylornithine (DFMO), a U.S. Food and Drug Administration (FDA) approved drug. We report two X-ray structures of ODC complexed with new ODC inhibitors, computational docking, molecular dynamics, and binding free energy calculations to validate the experimental models. The X-ray structures reveal that covalent adducts with pyridoxal phosphate (PLP) are formed in the active site of the human ODC enzyme, as verified by their preparation and enzymatic testing. Finally, we verified that the cellular activity of endogenous ODC was inhibited, and polyamine levels were reduced. Given that ODC is a clinically validated target, combined with the fact that DFMO is currently the only ODC inhibitor in clinical use for several indications, the further development of more potent ODC inhibitors with superior activity and physical properties is warranted.

60 APPLIED LIFE SCIENCES↗

DOE OSTI2022

First Fluorescent Acetylspermidine Deacetylation Assay for HDAC10 Identifies Selective Inhibitors with Cellular Target Engagement**

Abstract Histone deacetylases (HDACs) are important epigenetic regulators involved in many diseases, especially cancer. Five HDAC inhibitors have been approved for anticancer therapy and many are in clinical trials. Among the 11 zinc‐dependent HDACs, HDAC10 has received relatively little attention by drug discovery campaigns, despite its involvement, e. g., in the pathogenesis of neuroblastoma. This is due in part to a lack of robust enzymatic conversion assays. In contrast to the protein lysine deacetylase and deacylase activity of most other HDAC subtypes, it has recently been shown that HDAC10 has strong preferences for deacetylation of oligoamine substrates like acetyl‐putrescine or ‐spermidine. Hence, it is also termed a polyamine deacetylase (PDAC). Here, we present the first fluorescent enzymatic conversion assay for HDAC10 using an aminocoumarin‐labelled acetyl‐spermidine derivative to measure its PDAC activity, which is suitable for high‐throughput screening. Using this assay, we identified potent inhibitors of HDAC10‐mediated spermidine deacetylation in vitro. Based on the oligoamine preference of HDAC10, we also designed inhibitors with a basic moiety in appropriate distance to the zinc binding hydroxamate that showed potent inhibition of HDAC10 with high selectivity, and we solved a HDAC10‐inhibitor structure using X‐ray crystallography. We could demonstrate selective cellular target engagement for HDAC10 but a lysosomal phenotype in neuroblastoma cells that was previously associated with HDAC10 inhibition was not observed. Thus, we have developed new chemical probes for HDAC10 that allow further clarification of the biological role of this enzyme.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2025

Generalizable Porous Aromatic Framework‐Included Polymer Membranes for Diffusion‐Enhanced Gas Separations

Industrial separation processes account for 10-15% of global energy consumption. Membrane-based processes are less energy-intensive than traditional gas separation technologies; however, enhanced material separation performance and stability for numerous gas mixtures are needed for widespread industrial adoption. This work presents a generalizable strategy for preparing mixed-matrix gas separation membranes exceeding the performance upper bounds of existing polymer membranes for a wide variety of industrial gases. By incorporating robust porous aromatic framework (PAF) particles into various dense commercial polymer matrices, gas diffusivity and solubility can be enhanced. For diverse gas mixtures (e.g., CO2/N2, O2/N2, He/CH4, H2/N2, and C2H4/C2H6), the resulting composite membranes exhibit enhanced gas permeabilities-by as much as 520%-and largely unchanged selectivities even after 6 years of aging under simulated flue gas conditions. These improvements arise from the ultrahigh porosity, excellent chemical compatibility, and unique physicochemical properties of the embedded PAF particles. Functionalizing the PAFs with polyamines also enables composite membranes that achieve among the highest reported performances against plasticization, a common obstacle in commercializing gas separation membranes. Significantly, the PAF-1 particles are readily dispersible in various common membrane casting solvents, suggesting their broader utility as a filler for designing high-performance membranes for many industrial gas separations.

Uliana, Adam A↗

DOE OSTI2020

Recent advances in polymeric facilitated transport membranes for carbon dioxide separation and hydrogen purification

Membrane and membrane process have been widely considered as one of the best candidates for mitigating CO 2 emissions from the combustion or utilization of fossil fuels. Various amine-containing polymers constitute an important class of membranes, where the highly selective CO 2 transport is achieved by the facilitated transport mechanism. In this review, the amine–CO 2 chemistry is discussed in conjunction with the mechanism of the reaction-mediated CO 2 transport. A wide variety of amine-containing polymers are discussed based on two synthesis motifs: (a) polyamines with amino groups covalently bound to the polymer backbone and (b) small molecule amines embedded in a polymer matrix. This review concludes with the remarks on the facilitated transport membranes for post-combustion carbon capture (CO 2 /N 2 ) and hydrogen purification (CO 2 /H 2 ).

42 ENGINEERING↗

DOE OSTI2025

The structural basis for the broad aldehyde specificity of the aminoaldehyde dehydrogenase PauC from the human pathogen Pseudomonas aeruginosa

Abstract Despite significant differences in size and formal charge, the aldehyde dehydrogenasePaPauC (PA5312) fromPseudomonas aeruginosaPAO1 efficiently catalyzes the NAD + ‐dependent oxidation of the aminoaldehydes formed in polyamines degradation. We report here thatPaPauC also oxidizes 4‐guanidinebutyraldehyde, formed in one arginine degradation pathway, trimethylaminobutyraldehyde, of unknown metabolic origin, and indole‐3‐acetaldehyde, a precursor of the plant growth‐promoting hormone indoleacetic acid.PaPauC has been proposed as a potential target for combatingP. aeruginosa. However, understanding its structure–function relationships, crucial for developing specific inhibitors, is lacking. Using X‐ray crystallography, we identified the structural characteristics that determinePaPauC broad aldehyde specificity: a spacious aldehyde‐entrance tunnel and six active‐site residues. Docking simulations, site‐directed mutagenesis, and kinetic analyses support the interactions of Lys479 with glutamylated aminoaldehydes; Phe169, Trp176, and Phe467 with amino and guanidinium groups through cation–π interactions and with the indole group via NH–π and CH–π interactions; Asp459 with amino and indole groups; and Thr303 with amide and guanidinium groups. Exploiting the distinctive structural features of thePaPauC active site could aid in developing specific inhibitors to combatP. aeruginosainfections in humans and animals, as well as in preventing its colonization of plants, which are abundantP. aeruginosareservoirs and, therefore, a significant source of human infections.

Biochemistry & Molecular Biology↗

DOE OSTI2022

Sequential polymer infusion into solid substrates (SPISS): Impact of processing on sorbent CO 2 adsorption properties

Solid sorbents made of small amine molecules and polyamines infused into mesoporous substrates are promising materials for CO 2 capture technologies. To date, their preparation is mainly based on wet infusion with focus on increasing amine content by varying the structure of the amine sorbent and designing solid substrates of various pore parameters. Less explored in the field are changes in processing to afford efficient CO 2 sorbents. In this study, branched poly(ethylenimine) (bPEI, M w = 800 Da) alone and blends with linear poly(propylenimine) (LPPI, M n = 6,700 Da) are infused into solid SBA-15 substrates by a method that varies the solution processing called sequential polymer infusion into solid substrates (SPISS). The reference 40 % bPEI-SBA-15 samples are split by two methods: split batch in dry suspension (SBD) and split batch in liquid suspension (SBL). Sequentially, alcoholic 10% of bPEI (non-blends) and 10% of LPPI (blends) solutions are introduced to afford the desired products. Under dry conditions, the resulting 50% bPEI-SBA-15 SBD & SBL sorbents display high CO 2 capacities up to 3.47 mmol CO 2 /g SiO 2 for simulated flue gas (10% CO 2 ) and 2.62 mmol CO 2 /g SiO 2 for direct air capture (DAC, 400 ppm CO 2 ). Under humid DAC conditions the CO 2 performance is further enhanced with an uptake of 4.62 mmol CO 2 /gSiO 2 and amine efficiency of 0.22 mmol CO 2 /mmol N. Subjected to extended temperature swing adsorption kinetic cycling (20 cycles), the SPISS samples display stable working capacities and retain over 70% (blends) and over 90% (non-blends) of their initial 12 h adsorption performance. LPPI is demonstrated to be an effective water sorption limiting agent using dynamic vapor sorption measurements. Solid state NMR techniques reveal important insights into the dynamics of the amine polymers confined into SBA-15 pores, as impacted by processing conditions. The results suggest that the conformation of the polymers is different depending on the processing method, displaying relatively tight (SBD) and loose (SBL) packing. Finally, the simple solution processing approaches presented here show that processing variations may guide the design of solid amine sorbents with desirable properties relevant for integration into CO 2 capture technologies.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2021

Assessment of Plant and Microalgal Oil-Derived Nonisocyanate Polyurethane Products for Potential Commercialization

Green pathways for nonisocyanate polyurethane (NIPU) production have attracted increasing levels of interest. The reaction between 5-membered cyclic carbonate and polyamines is one of the most promising pathways to produce NIPU polymers. Though promising, major technical hurdles such as slow polymerization rate and poor performance hinder the commercialization of NIPU. In this paper, we screened several commercially available triglyceride oil feedstocks for NIPU products, focusing on polymerization kinetics and product performance for industrial application. The impact of carbonated group density on polymerization rate and mechanical strength was determined. We have demonstrated a remarkably higher reactivity of carbonated oil derived from feedstocks with polyunsaturated fatty acid (PUFA). The NIPU derived from such feedstocks also showed improved performance for industrial application. Unlike traditional polyurethane foam production that uses isocyanate and water to generate CO2 as a blowing reagent, there is no gas formation in NIPU polymerization. We have demonstrated a practical and cost-effective approach to produce NIPU foam material using bicarbonate as a blowing reagent. Furthermore, we conducted the first-ever technoeconomic analysis (TEA), revealing that profitable commercial NIPU production can be achieved when operating at sufficient production capacities.

09 BIOMASS FUELS↗

DOE OSTI2025

Mesh-like structure integrated core-shell-shell nanocomposites for enhanced stability and performance in carbon capture

Carbon capture is essential for mitigating climate change, yet most sorbents struggle to combine high capacity with chemical stability. Here we report core-shell-shell (CSS) nanocomposites that integrate adsorption efficiency with exceptional robustness. The design couples a metal-organic framework (MOF) core, which enriches local CO 2 concentration, with a polyamine shell that is reorganized into a porous, ordered network through entanglement with an outer covalent organic framework (COF) shell. This hierarchical architecture enables dual amine functionalization via sequential “click” and Schiff-base reactions, achieving a CO 2 uptake of 3.4 mmol g −1 at 1 bar. The COF outer layer also acts as a protective barrier, suppressing humidity interference and doubling cycling stability under simulated flue gas. Remarkably, the nanocomposites maintain structural integrity after one week in strongly acidic (3 M HNO 3 ) or basic (NaOH, pH=14) environments, underscoring their chemical resilience. By uniting high capacity, cycling durability, and environmental tolerance, this CSS strategy offers a versatile platform for next-generation carbon capture materials.

Yang, Sizhuo [Lawrence Berkeley National Laborator↗

DOE OSTI2021

Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface

General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNATs) catalyse the acetylation of a diverse range of substrates, thereby orchestrating a variety of biological processes within prokaryotes and eukaryotes. GNAT enzymes can catalyze the transfer of an acetyl group from acetyl coenzyme A to substrates such as aminoglycoside antibiotics, amino acids, polyamines, peptides, vitamins, catecholamines, and large macromolecules including proteins. Although GNATs generally exhibit low to moderate sequence identity, they share a conserved catalytic fold and conserved structural motifs. In this current study we characterize the high-resolution X-ray crystallographic structure of a GNAT enzyme bound with acetyl-CoA from Elizabethkingia anophelis , an important multi-drug resistant bacterium. The tertiary structure is comprised of six α-helices and nine β-strands, and is similar with other GNATs. We identify a new and uncharacterized GNAT dimer interface, which is conserved in at least two other unpublished GNAT structures. This suggests that GNAT enzymes can form at least five different types of dimers, in addition to a range of other oligomers including trimer, tetramer, hexamer, and dodecamer assemblies. The high-resolution structure presented in this study is suitable for future in-silico docking and structure–activity relationship studies.

59 BASIC BIOLOGICAL SCIENCES↗

DOE OSTI2022

Structure of the human cation–chloride cotransport KCC1 in an outward-open state

Cation–chloride cotransporters (CCCs) catalyze electroneutral symport of Cl - with Na + and/or K + across membranes. CCCs are fundamental in cell volume homeostasis, transepithelia ion movement, maintenance of intracellular Cl - concentration, and neuronal excitability. Here, we present a cryoelectron microscopy structure of human K + –Cl - cotransporter (KCC)1 bound with the VU0463271 inhibitor in an outward-open state. In contrast to many other amino acid–polyamine–organocation transporter cousins, our first outward-open CCC structure reveals that opening the KCC1 extracellular ion permeation path does not involve hinge-bending motions of the transmembrane (TM) 1 and TM6 half-helices. Instead, rocking of TM3 and TM8, together with displacements of TM4, TM9, and a conserved intracellular loop 1 helix, underlie alternate opening and closing of extracellular and cytoplasmic vestibules. We show that KCC1 intriguingly exists in one of two distinct dimeric states via different intersubunit interfaces. Our studies provide a blueprint for understanding the mechanisms of CCCs and their inhibition by small molecule compounds.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗

DOE OSTI2021

Alternative pathways utilize or circumvent putrescine for biosynthesis of putrescine-containing rhizoferrin

The siderophore rhizoferrin (N 1 ,N 4 -dicitrylputrescine) is produced in fungi and bacteria to scavenge iron. Putrescine-producing bacterium Ralstonia pickettii synthesizes rhizoferrin and encodes a single nonribosomal peptide synthetase-independent siderophore (NIS) synthetase. From biosynthetic logic, we hypothesized that this single enzyme is sufficient for rhizoferrin biosynthesis. We confirmed this by expression of R. pickettii NIS synthetase in Escherichia coli, resulting in rhizoferrin production. This was further confirmed in vitro using the recombinant NIS synthetase, synthesizing rhizoferrin from putrescine and citrate. Heterologous expression of homologous lbtA from Legionella pneumophila, required for rhizoferrin biosynthesis in that species, produced siderophore activity in E. coli. Rhizoferrin is also synthesized by Francisella tularensis and Francisella novicida, but unlike R. pickettii or L. pneumophila, Francisella species lack putrescine biosynthetic pathways because of genomic decay. Francisella encodes a NIS synthetase FslA/FigA and an ornithine decarboxylase homolog FslC/FigC, required for rhizoferrin biosynthesis. Ornithine decarboxylase produces putrescine from ornithine, but we show here in vitro that FigA synthesizes N-citrylornithine, and FigC is an N-citrylornithine decarboxylase that together synthesize rhizoferrin without using putrescine. We co-expressed F. novicida figA and figC in E. coli and produced rhizoferrin. A 2.1 Å X-ray crystal structure of the FigC N-citrylornithine decarboxylase reveals how the larger substrate is accommodated and how active site residues have changed to recognize N-citrylornithine. FigC belongs to a new subfamily of alanine racemase-fold PLP-dependent decarboxylases that are not involved in polyamine biosynthesis. These data reveal a natural product biosynthetic workaround that evolved to bypass a missing precursor and re-establish it in the final structure.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗