Log in

Relevant bibliographies by topics / Aminopeptidases Design / Journal articles

Journal articles on the topic 'Aminopeptidases Design'

To see the other types of publications on this topic, follow the link: Aminopeptidases Design.

Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Aminopeptidases Design.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Malcolm, Tess R., Karolina W. Swiderska, Brooke K. Hayes, Chaille T. Webb, Marcin Drag, Nyssa Drinkwater, and Sheena McGowan. "Mapping the substrate specificity of the Plasmodium M1 and M17 aminopeptidases." Biochemical Journal 478, no. 13 (July 16, 2021): 2697–713. http://dx.doi.org/10.1042/bcj20210172.

Full text

Abstract:

During malarial infection, Plasmodium parasites digest human hemoglobin to obtain free amino acids for protein production and maintenance of osmotic pressure. The Plasmodium M1 and M17 aminopeptidases are both postulated to have an essential role in the terminal stages of the hemoglobin digestion process and are validated drug targets for the design of new dual-target anti-malarial compounds. In this study, we profiled the substrate specificity fingerprints and kinetic behaviors of M1 and M17 aminopeptidases from Plasmodium falciparum and Plasmodium vivax, and the mouse model species, Plasmodium berghei. We found that although the Plasmodium M1 aminopeptidases share a largely similar, broad specificity at the P1 position, the P. falciparum M1 displays the greatest diversity in specificity and P. berghei M1 showing a preference for charged P1 residues. In contrast, the Plasmodium M17 aminopeptidases share a highly conserved preference for hydrophobic residues at the P1 position. The aminopeptidases also demonstrated intra-peptide sequence specificity, particularly the M1 aminopeptidases, which showed a definitive preference for peptides with fewer negatively charged intrapeptide residues. Overall, the P. vivax and P. berghei enzymes had a faster substrate turnover rate than the P. falciparum enzymes, which we postulate is due to subtle differences in structural dynamicity. Together, these results build a kinetic profile that allows us to better understand the catalytic nuances of the M1 and M17 aminopeptidases from different Plasmodium species.

APA, Harvard, Vancouver, ISO, and other styles

2

Mahon, Cathal S., Anthony J. O'Donoghue, David H. Goetz, Patrick G. Murray, Charles S. Craik, and Maria G. Tuohy. "Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii." Microbiology 155, no. 11 (November 1, 2009): 3673–82. http://dx.doi.org/10.1099/mic.0.030940-0.

Full text

Abstract:

Fungi are capable of degrading proteins in their environment by secreting peptidases. However, the link between extracellular digestion and intracellular proteolysis has scarcely been investigated. Mycelial lysates of the filamentous fungus Talaromyces emersonii were screened for intracellular peptidase production. Five distinct proteolytic activities with specificity for the p-nitroanilide (pNA) peptides Suc-AAPF-pNA, Suc-AAA-pNA, K-pNA, F-pNA and P-pNA were identified. The native enzyme responsible for the removal of N-terminal proline residues was purified to homogeneity by ammonium sulfate fractionation followed by five successive chromatographic steps. The enzyme, termed Talaromyces emersonii prolyl aminopeptidase (TePAP), displayed a 50-fold specificity for cleaving N-terminal Pro–X (k cat/K m=2.1×106 M−1 s−1) compared with Ala–X or Val–X bonds. This intracellular aminopeptidase was optimally active at pH 7.4 and 50 °C. Peptide sequencing facilitated the design of degenerate oligonucleotides from homologous sequences encoding putative fungal proline aminopeptidases, enabling subsequent cloning of the gene. TePAP was shown to be relatively uninhibited by classical serine peptidase inhibitors and to be sensitive to selected cysteine- and histidine-modifying reagents, yet gene sequence analysis identified the protein as a serine peptidase with an α/β hydrolase fold. Northern analysis indicated that Tepap mRNA levels were regulated by the composition of the growth medium. Highest Tepap transcript levels were observed when the fungus was grown in medium containing glucose and the protein hydrolysate casitone. Interestingly, both the induction profile and substrate preference of this enzyme suggest potential co-operativity between extracellular and intracellular proteolysis in this organism. Gel filtration chromatography suggested that the enzyme exists as a 270 kDa homo-hexamer, whereas most bacterial prolyl aminopeptidases (PAPs) are monomers. Phylogenetic analysis of known PAPs revealed two diverse subfamilies that are distinguishable on the basis of primary and secondary structure and appear to correlate with the subunit composition of the native enzymes. Sequence comparisons revealed that PAPs with key conserved topological features are widespread in bacterial and fungal kingdoms, and this study identified many putative PAP candidates within sequenced genomes. This work represents, to our knowledge, the first detailed biochemical and molecular analysis of an inducible PAP from a eukaryote and the first intracellular peptidase isolated from the thermophilic fungus T. emersonii.

APA, Harvard, Vancouver, ISO, and other styles

3

Tsoukalidou, Sofia, Magdalini Kakou, Ioannis Mavridis, Despoina Koumantou, Vito Calderone, Marco Fragai, Efstratios Stratikos, Athanasios Papakyriakou, and Dionisios Vourloumis. "Exploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases." Bioorganic & Medicinal Chemistry 27, no. 24 (December 2019): 115177. http://dx.doi.org/10.1016/j.bmc.2019.115177.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Gordon, E. M., J. D. Godfrey, N. G. Delaney, M. M. Asaad, D. Von Langen, and D. W. Cushman. "Design of novel inhibitors of aminopeptidases. Synthesis of peptide-derived diamino thiols and sulfur replacement analogs of bestatin." Journal of Medicinal Chemistry 31, no. 11 (November 1988): 2199–211. http://dx.doi.org/10.1021/jm00119a023.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Tholander, Fredrik, Ayumo Muroya, Bernard-Pierre Roques, Marie-Claude Fournié-Zaluski, Marjolein M. G. M. Thunnissen, and Jesper Z. Haeggström. "Structure-Based Dissection of the Active Site Chemistry of Leukotriene A4 Hydrolase: Implications for M1 Aminopeptidases and Inhibitor Design." Chemistry & Biology 15, no. 9 (September 2008): 920–29. http://dx.doi.org/10.1016/j.chembiol.2008.07.018.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Wanat, Weronika, Michał Talma, Błażej Dziuk, and Paweł Kafarski. "Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases." Biomolecules 10, no. 9 (September 14, 2020): 1319. http://dx.doi.org/10.3390/biom10091319.

Full text

Abstract:

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors of both enzymes. To the best of our knowledge, P1 homophenylalanine analogues are the most active inhibitors of the APN among phosphonic and phosphinic derivatives described in the literature. Therefore, they constitute interesting building blocks for the further design of chemically more complex inhibitors. Based on molecular modeling simulations and SAR (structure-activity relationship) analysis, the optimal architecture of enzyme-inhibitor complexes for hAPN and pAPN were determined.

APA, Harvard, Vancouver, ISO, and other styles

7

Irfan, Iram, Asghar Ali, Bharati Reddi, Mohd Abrar Khan, Phool Hasan, Sarfraz Ahmed, Amad Uddin, et al. "Design, Synthesis and Mechanistic Studies of Novel Isatin-Pyrazole Hydrazone Conjugates as Selective and Potent Bacterial MetAP Inhibitors." Antibiotics 11, no. 8 (August 19, 2022): 1126. http://dx.doi.org/10.3390/antibiotics11081126.

Full text

Abstract:

Methionine aminopeptidases (MetAPs) are attractive drug targets due to their essential role in eukaryotes as well as prokaryotic cells. In this study, biochemical assays were performed on newly synthesized Isatin-pyrazole hydrazones (PS1–14) to identify potent and selective bacterial MetAPs inhibitors. Compound PS9 inhibited prokaryotic MetAPs, i.e., MtMetAP1c, EfMetAP1a and SpMetAP1a with Ki values of 0.31, 6.93 and 0.37 µM, respectively. Interestingly, PS9 inhibited the human analogue HsMetAP1b with Ki (631.7 µM) about ten thousand-fold higher than the bacterial MetAPs. The in vitro screening against Gram-positive (Enterococcus faecalis, Bacillus subtilis and Staphylococcus aureus) and Gram-negative (Pseudomonas aeruginosa, Klebsiella pneumonia and Escherichia coli) bacterial strains also exhibited their antibacterial potential supported by minimum bactericidal concentration (MBC), disk diffusion assay, growth curve and time-kill curve experiments. Additionally, PS6 and PS9 had synergistic effects when combined with ampicillin (AMP) and ciprofloxacin (CIP) against selective bacterial strains. PS9 showed no significant cytotoxic effect on human RBCs, HEK293 cells and Galleria mellonella larvae in vivo. PS9 inhibited the growth of multidrug-resistant environmental isolates as it showed the MIC lower than the standard drugs used against selective bacterial strains. Overall, the study suggested PS9 could be a useful candidate for the development of antibacterial alternatives.

APA, Harvard, Vancouver, ISO, and other styles

8

Reid, A., A. Protheroe, G. Attard, C. Cowsill, J. Spicer, L. Vidal, E. Bone, L. Hooftman, A. Harris, and J. S. De-Bono. "A phase 1 dose finding study of CHR-2797, an inhibitor of M1 aminopeptidases, in patients with advanced solid tumours." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 3053. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.3053.

Full text

Abstract:

3053 Background: CHR-2797 is a novel, orally bioavailable inhibitor of the M1 family of aminopeptidases, in particular PuSA, and LTA4 hydrolase. Exposure of cancer cells to CHR-2797 results in the generation of the active metabolite CHR-79888 which is poorly membrane-permeable, resulting in intracellular accumulation. CHR-2797 has shown anti-proliferative activity in syngeneic (rat) and xenograft (mouse) cancer models, and is anti-angiogenic in vitro. Methods: Patients (pts) (ECOG PS ≤ 2) with histologically confirmed advanced solid tumors resistant or refractory to standard therapy were eligible. The accelerated titration design of the trial involved two phases for evaluation of schedule and dose: 1) fixed dose with increasing duration, and 2) dose escalation over a fixed duration (28 days). Results: 16 pts (median age: 64.5 years [range 48.8–80.1], 13M/3F)were treated with once daily doses ranging from 10mg to 130mg. The first four patients received a 10mg dose for 7, 14, 21 or 28 days respectively. Five subsequent cohorts received 28 days continuous dosing, with dose doubling in single patient cohorts until drug-related toxicity ≥ Grade 2. Thereafter dose was escalated in ≤ 40% increments in 3-patient cohorts. The most frequent adverse events were: gr 1–2 thrombocytopenia (44%), gr 1 diarrhea (25%), gr 1–2 transaminitis (19%), gr 1–2 fatigue (13%), gr 1 hot flushes (13%), and gr 1 lightheadedness (13%). There were no DLTs. Five patients continued therapy after 28 days; stable disease has been achieved in 1 pt for 6 months with granulosa cell carcinoma of ovary, who was progressing prior to study entry. CHR-2797 and CHR-79888 demonstrate dose proportional increases in AUC and Cmax. The terminal half-life for CHR-2797 is around 1–2 hours, whereas it is between 9 and 11 hours for CHR-79888. Intracellular (packed blood cells) exposure to both CHR-2797 and CHR-79888 is good, with CHR-79888 accumulating over 28 days, such that by day 28 the intracellular levels are comparable to plasma. Conclusions: CHR-2797 is well tolerated and can be safely administered at doses that reach plasma concentrations associated with activity in pre-clinical models. Accrual into the study continues. No significant financial relationships to disclose.

APA, Harvard, Vancouver, ISO, and other styles

9

Protheroe, A., A. Reid, G. Attard, A. Davies, J. Spicer, L. Vidal, E. Bone, L. Hooftman, A. Harris, and J. De-Bono. "First in-human phase 1 trial of a novel amino-peptidase inhibitor, CHR-2797." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 3537. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.3537.

Full text

Abstract:

3537 Background: CHR-2797 is a novel, orally bioavailable agent which displays potent, tumor cell-selective, anti-proliferative properties. It is an inhibitor of Zn++-dependent aminopeptidases and generates signs of amino acid deprivation in sensitive cells, decreased protein synthesis and an increase in the level of the pro-apoptotic protein, Noxa. CHR-79888 is an active metabolite of CHR-2797. Patients and Methods: This study was conducted according to an accelerated titration design to define the MTD, DLT, toxicity profile and PK of CHR-2797 when administered orally for 28 days or longer. Patients (ECOG PS = 2) with histologically confirmed advanced solid tumors resistant or refractory to standard therapy were eligible. Results: 37 pts (median age 61.5 years [range 22.4–80.1]; 30M/7F; median ECOG PS 1; median prior regimens 2, range 0–6) enrolled in 12 cohorts (doses between 10 and 320mg). The first four patients received a 10 mg dose for 7, 14, 21 or 28 days respectively. Subsequent cohorts received 28 days continuous dosing, with dose doubling in single patient cohorts until drug-related toxicity = Grade 2. Thereafter the study followed a 3+3 design with = 40% dose increments. Common (gr 1–2) toxicity included fatigue (47%), diarrhea (47%), dizziness (24%), constipation, vomiting, abdominal pain (all 21%), and thrombocytopenia (18%). Toxicities show dose dependency for thrombocytopenia and fatigue. MTD was declared at 320 mg after 2 DLT’s were reported: 2 patients were unable to complete 28 days of daily dosing due to syncope/anemia, and dizziness/visual disturbances/thrombocytopenia, respectively. Patients recovered fully after cessation of the drug. The dose level below (240 mg) was expanded to 13 patients. Plasma PK was determined for both CHR-2797 and -79888, on days 1 and 28, which showed dose proportional increases in AUC and Cmax. Intracellular and intratumoral levels of both the parent and metabolite were also measured. So far 4 patients continued therapy for 7–9 months: one patient (RCC [130 mg]) achieved a PR, and 3 patients (ovarian ca [40 mg], NSCLC [130 mg], and breast ca [180 mg] had confirmed SD (> 3 months). Conclusion: Once daily oral CHR-2797 can be administered safely for 28 days in doses up to 240 mg and exhibits favorable PK. No significant financial relationships to disclose.

APA, Harvard, Vancouver, ISO, and other styles

10

Grembecka, J., and P. Kafarski. "Leucine Aminopeptidase as a Target for Inhibitor Design." Mini-Reviews in Medicinal Chemistry 1, no. 2 (July 1, 2001): 133–44. http://dx.doi.org/10.2174/1389557013406990.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

He, Xinyuan, Yiming Hu, Wen Shi, Xiaohua Li, and Huimin Ma. "Design, synthesis and application of a near-infrared fluorescent probe for in vivo imaging of aminopeptidase N." Chemical Communications 53, no. 68 (2017): 9438–41. http://dx.doi.org/10.1039/c7cc05142e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Amin, Sk Abdul, Nilanjan Adhikari, and Tarun Jha. "Design of Aminopeptidase N Inhibitors as Anti-cancer Agents." Journal of Medicinal Chemistry 61, no. 15 (April 9, 2018): 6468–90. http://dx.doi.org/10.1021/acs.jmedchem.7b00782.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Ziemska, Joanna, Jolanta Solecka, and Małgorzata Jarończyk. "In Silico Screening for Novel Leucine Aminopeptidase Inhibitors with 3,4-Dihydroisoquinoline Scaffold." Molecules 25, no. 7 (April 10, 2020): 1753. http://dx.doi.org/10.3390/molecules25071753.

Full text

Abstract:

Cancers are the leading cause of deaths worldwide. In 2018, an estimated 18.1 million new cancer cases and 9.6 million cancer-related deaths occurred globally. Several previous studies have shown that the enzyme, leucine aminopeptidase is involved in pathological conditions such as cancer. On the basis of the knowledge that isoquinoline alkaloids have antiproliferative activity and inhibitory activity towards leucine aminopeptidase, the present study was conducted a study which involved database search, virtual screening, and design of new potential leucine aminopeptidase inhibitors with a scaffold based on 3,4-dihydroisoquinoline. These compounds were then filtered through Lipinski’s “rule of five,” and 25 081 of them were then subjected to molecular docking. Next, three-dimensional quantitative structure-activity relationship (3D-QSAR) study was performed for the selected group of compounds with the best binding score results. The developed model, calculated by leave-one-out method, showed acceptable predictive and descriptive capability as represented by standard statistical parameters r2 (0.997) and q2 (0.717). Further, 35 compounds were identified to have an excellent predictive reliability. Finally, nine selected compounds were evaluated for drug-likeness and different pharmacokinetics parameters such as absorption, distribution, metabolism, excretion, and toxicity. Our methodology suggested that compounds with 3,4-dihydroisoquinoline moiety were potentially active in inhibiting leucine aminopeptidase and could be used for further in-depth in vitro and in vivo studies.

APA, Harvard, Vancouver, ISO, and other styles

14

Georgiadis, Dimitris, Anastasia Mpakali, Despoina Koumantou, and Efstratios Stratikos. "Inhibitors of ER Aminopeptidase 1 and 2: From Design to Clinical Application." Current Medicinal Chemistry 26, no. 15 (July 25, 2019): 2715–29. http://dx.doi.org/10.2174/0929867325666180214111849.

Full text

Abstract:

Endoplasmic Reticulum aminopeptidase 1 and 2 are two homologous enzymes that help generate peptide ligands for presentation by Major Histocompatibility Class I molecules. Their enzymatic activity influences the antigenic peptide repertoire and indirectly controls adaptive immune responses. Accumulating evidence suggests that these two enzymes are tractable targets for the regulation of immune responses with possible applications ranging from cancer immunotherapy to treating inflammatory autoimmune diseases. Here, we review the state-of-the-art in the development of inhibitors of ERAP1 and ERAP2 as well as their potential and limitations for clinical applications.

APA, Harvard, Vancouver, ISO, and other styles

15

Barlow, Nicholas, Sudarsana Reddy Vanga, Jonas Sävmarker, Anja Sandström, Peta Burns, Anders Hallberg, Johan Åqvist, et al. "Macrocyclic peptidomimetics as inhibitors of insulin-regulated aminopeptidase (IRAP)." RSC Medicinal Chemistry 11, no. 2 (2020): 234–44. http://dx.doi.org/10.1039/c9md00485h.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Zhang, Xiaopan, and Wenfang Xu. "Aminopeptidase N (APN/CD13) as a Target for Anti-Cancer Agent Design." Current Medicinal Chemistry 15, no. 27 (November 1, 2008): 2850–65. http://dx.doi.org/10.2174/092986708786242840.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Hata, Ryunosuke, Hiroshi Nonaka, Yoichi Takakusagi, Kazuhiro Ichikawa, and Shinsuke Sando. "Design of a Hyperpolarized Molecular Probe for Detection of Aminopeptidase N Activity." Angewandte Chemie 128, no. 5 (December 21, 2015): 1797–800. http://dx.doi.org/10.1002/ange.201509457.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Hata, Ryunosuke, Hiroshi Nonaka, Yoichi Takakusagi, Kazuhiro Ichikawa, and Shinsuke Sando. "Design of a Hyperpolarized Molecular Probe for Detection of Aminopeptidase N Activity." Angewandte Chemie International Edition 55, no. 5 (January 26, 2016): 1765–68. http://dx.doi.org/10.1002/anie.201509457.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Kumar, Amit, Gopal Raj Periyannan, Beena Narayanan, Aaron W. Kittell, Jung-Ja Kim, and Brian Bennett. "Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus." Biochemical Journal 403, no. 3 (April 12, 2007): 527–36. http://dx.doi.org/10.1042/bj20061591.

Full text

Abstract:

Metallohydrolases catalyse some of the most important reactions in biology and are targets for numerous chemotherapeutic agents designed to combat bacterial infectivity, antibiotic resistance, HIV infectivity, tumour growth, angiogenesis and immune disorders. Rational design of inhibitors of these enzymes with chemotherapeutic potential relies on detailed knowledge of the catalytic mechanism. The roles of the catalytic transition ions in these enzymes have long been assumed to include the activation and delivery of a nucleophilic hydroxy moiety. In the present study, catalytic intermediates in the hydrolysis of L-leucyl-L-leucyl-L-leucine by Vibrio proteolyticus aminopeptidase were characterized in spectrokinetic and structural studies. Rapid-freeze-quench EPR studies of reaction products of L-leucyl-L-leucyl-L-leucine and Co(II)-substituted aminopeptidase, and comparison of the EPR data with those from structurally characterized complexes of aminopeptidase with inhibitors, indicated the formation of a catalytically competent post-Michaelis pre-transition state intermediate with a structure analogous to that of the inhibited complex with bestatin. The X-ray crystal structure of an aminopeptidase–L-leucyl-L-leucyl-L-leucine complex was also analogous to that of the bestatin complex. In these structures, no water/hydroxy group was observed bound to the essential metal ion. However, a water/hydroxy group was clearly identified that was bound to the metal-ligating oxygen atom of Glu152. This water/hydroxy group is proposed as a candidate for the active nucleophile in a novel metallohydrolase mechanism that shares features of the catalytic mechanisms of aspartic proteases and of B2 metallo-β-lactamases. Preliminary studies on site-directed variants are consistent with the proposal. Other features of the structure suggest roles for the dinuclear centre in geometrically and electrophilically activating the substrate.

APA, Harvard, Vancouver, ISO, and other styles

20

Drag, Marcin, Jolanta Grembecka, and Paweł Kafarski. "The Computer-Aided Design, Synthesis, and Activity Prediction of New Leucine Aminopeptidase Inhibitors." Phosphorus, Sulfur, and Silicon and the Related Elements 177, no. 6-7 (June 1, 2002): 1591–95. http://dx.doi.org/10.1080/10426500212322.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Huixiong Chen, Bernard P. Roques, and Marie-Claude Fournié-Zaluski. "Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor." Bioorganic & Medicinal Chemistry Letters 9, no. 11 (June 1999): 1511–16. http://dx.doi.org/10.1016/s0960-894x(99)00219-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Flipo, Marian, Isabelle Florent, Philippe Grellier, Christian Sergheraert, and Rebecca Deprez-Poulain. "Design, synthesis and antimalarial activity of novel, quinoline-Based, zinc metallo-aminopeptidase inhibitors." Bioorganic & Medicinal Chemistry Letters 13, no. 16 (August 2003): 2659–62. http://dx.doi.org/10.1016/s0960-894x(03)00550-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Mou, Jiajia, Yepeng Luan, Danghui Chen, and Qiang Wang. "Novel L-arginine derivatives as aminopeptidase N inhibitors: design, chemistry, and pharmacological evaluation." Medicinal Chemistry Research 26, no. 11 (August 16, 2017): 3015–25. http://dx.doi.org/10.1007/s00044-017-1999-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Ma, Chunhua, Jiangying Cao, Xuewu Liang, Yongxue Huang, Ping Wu, Yingxia Li, Wenfang Xu, and Yingjie Zhang. "Novel leucine ureido derivatives as aminopeptidase N inhibitors. Design, synthesis and activity evaluation." European Journal of Medicinal Chemistry 108 (January 2016): 21–27. http://dx.doi.org/10.1016/j.ejmech.2015.11.021.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Grembecka, Jolanta, Artur Mucha, Tomasz Cierpicki, and Paweł Kafarski. "Structure-Based Design and Synthesis of Dipeptide Analogues as New Inhibitors of Leucine Aminopeptidase." Phosphorus, Sulfur, and Silicon and the Related Elements 177, no. 6-7 (June 1, 2002): 1739–43. http://dx.doi.org/10.1080/10426500212289.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Grembecka, Jolanta, Artur Mucha, Tomasz Cierpicki, and Paweł Kafarski. "The Most Potent Organophosphorus Inhibitors of Leucine Aminopeptidase. Structure-Based Design, Chemistry, and Activity." Journal of Medicinal Chemistry 46, no. 13 (June 2003): 2641–55. http://dx.doi.org/10.1021/jm030795v.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Li, Xun, Junli Wang, Lei Zhang, and Wenfang Xu. "Design, Synthesis, and Preliminary Activity Evaluation of Novel Peptidomimetics as Aminopeptidase N/CD13 Inhibitors." Archiv der Pharmazie 344, no. 8 (June 16, 2011): 494–504. http://dx.doi.org/10.1002/ardp.201100109.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Li, Qianbin, Hao Fang, Xuejian Wang, Gaoyun Hu, Qiang Wang, and Wenfang Xu. "Novel potent 2,5-pyrrolidinedione peptidomimetics as aminopeptidase N inhibitors. Design, synthesis and activity evaluation." Bioorganic & Medicinal Chemistry Letters 22, no. 2 (January 2012): 850–53. http://dx.doi.org/10.1016/j.bmcl.2011.12.048.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Žalubovskis, Raivis, and Jean-Yves Winum. "Inhibitors of Selected Bacterial Metalloenzymes." Current Medicinal Chemistry 26, no. 15 (July 25, 2019): 2690–714. http://dx.doi.org/10.2174/0929867325666180403154018.

Full text

Abstract:

The utilization of bacterial metalloenzymes, especially ones not having mammalian (human) counterparts, has drawn attention to develop novel antibacterial agents to overcome drug resistance and especially multidrug resistance. In this review, we focus on the recent achievements on the development of inhibitors of bacterial enzymes peptide deformylase (PDF), metallo-β-lactamase (MBL), methionine aminopeptidase (MetAP) and UDP-3-O-acyl- N-acetylglucosamine deacetylase (LpxC). The state of the art of the design and investigation of inhibitors of bacterial metalloenzymes is presented, and challenges are outlined and discussed.

APA, Harvard, Vancouver, ISO, and other styles

30

Liu, Shi-Yu, Huiling Wang, Xiaoting Zou, and Gang Nie. "De novo design of an ultrasensitive fluorogenic probe for aminopeptidase N sensing in living system." Sensors and Actuators B: Chemical 363 (July 2022): 131828. http://dx.doi.org/10.1016/j.snb.2022.131828.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Pan, Huili, Kanghui Yang, Jian Zhang, Yingying Xu, Yuqi Jiang, Yumei Yuan, Xiaopan Zhang, and Wenfang Xu. "Design, synthesis and biological evaluation of novel L-isoserine tripeptide derivatives as aminopeptidase N inhibitors." Journal of Enzyme Inhibition and Medicinal Chemistry 28, no. 4 (April 30, 2012): 717–26. http://dx.doi.org/10.3109/14756366.2012.680062.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Wang, Tianlin, Qi Sun, Huiwen Xiong, Chao Ma, Cuifen Lu, Junqi Nie, Guichun Yang, et al. "Rational design of fluorescent probes: Improving hydrophilicity, ratiometric and NIR trapping of endogenous leucine aminopeptidase." Sensors and Actuators B: Chemical 321 (October 2020): 128631. http://dx.doi.org/10.1016/j.snb.2020.128631.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Yang, Kanghui, Qiang Wang, Li Su, Hao Fang, Xuejian Wang, Jianzhi Gong, Binghe Wang, and Wenfang Xu. "Design and synthesis of novel chloramphenicol amine derivatives as potent aminopeptidase N (APN/CD13) inhibitors." Bioorganic & Medicinal Chemistry 17, no. 11 (June 2009): 3810–17. http://dx.doi.org/10.1016/j.bmc.2009.04.038.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Su, Li, Hao Fang, Kanghui Yang, Yingying Xu, and Wenfang Xu. "Design, synthesis and biological evaluation of novel l-lysine ureido derivatives as aminopeptidase N inhibitors." Bioorganic & Medicinal Chemistry 19, no. 2 (January 2011): 900–906. http://dx.doi.org/10.1016/j.bmc.2010.11.066.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Li, Qianbin, Hao Fang, Xuejian Wang, Liping Hu, and Wenfang Xu. "Novel cyclic-imide peptidomimetics as aminopeptidase N inhibitors. Design, chemistry and activity evaluation. Part I." European Journal of Medicinal Chemistry 44, no. 12 (December 2009): 4819–25. http://dx.doi.org/10.1016/j.ejmech.2009.07.022.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Chen, Huixiong, Bernard P. Roques, and Marie-Claude Fournie-Zaluski. "ChemInform Abstract: Design of the First Highly Potent and Selective Aminopeptidase N (EC 3.4.11.2) Inhibitor." ChemInform 30, no. 37 (June 13, 2010): no. http://dx.doi.org/10.1002/chin.199937216.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

González-Bacerio, Jorge, Irina Arocha, Mirtha Elisa Aguado, Yanira Méndez, Sabrina Marsiccobetre, Maikel Izquierdo, Daniel G. Rivera, Katherine Figarella, and Néstor L. Uzcátegui. "KBE009: A Bestatin-Like Inhibitor of the Trypanosoma cruzi Acidic M17 Aminopeptidase with In Vitro Anti-Trypanosomal Activity." Life 11, no. 10 (October 1, 2021): 1037. http://dx.doi.org/10.3390/life11101037.

Full text

Abstract:

Chagas disease, caused by the kinetoplastid parasite Trypanosoma cruzi, is a human tropical illness mainly present in Latin America. The therapies available against this disease are far from ideal. Proteases from pathogenic protozoan have been considered as good drug target candidates. T. cruzi acidic M17 leucyl-aminopeptidase (TcLAP) mediates the major parasite’s leucyl-aminopeptidase activity and is expressed in all parasite stages. Here, we report the inhibition of TcLAP (IC50 = 66.0 ± 13.5 µM) by the bestatin-like peptidomimetic KBE009. This molecule also inhibited the proliferation of T. cruzi epimastigotes in vitro (EC50 = 28.1 ± 1.9 µM) and showed selectivity for the parasite over human dermal fibroblasts (selectivity index: 4.9). Further insight into the specific effect of KBE009 on T. cruzi was provided by docking simulation using the crystal structure of TcLAP and a modeled human orthologous, hLAP3. The TcLAP-KBE009 complex is more stable than its hLAP3 counterpart. KBE009 adopted a better geometrical shape to fit into the active site of TcLAP than that of hLAP3. The drug-likeness and lead-likeness in silico parameters of KBE009 are satisfactory. Altogether, our results provide an initial insight into KBE009 as a promising starting point compound for the rational design of drugs through further optimization.

APA, Harvard, Vancouver, ISO, and other styles

38

Wang, Qiang, Fuming Xu, Jiajia Mou, Jian Zhang, Luqing Shang, Yepeng Luan, Yumei Yuan, et al. "Design, Synthesis and Preliminary Activity Evaluation of Novel L-Lysine Derivatives as Aminopeptidase N/CD13 Inhibitors." Protein & Peptide Letters 17, no. 7 (July 1, 2010): 847–53. http://dx.doi.org/10.2174/092986610791306661.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Kishor, Chandan, Rajesh Gumpena, Ravikumar Reddi, and Anthony Addlagatta. "Structural studies of Enterococcus faecalis methionine aminopeptidase and design of microbe specific 2,2′-bipyridine based inhibitors." MedChemComm 3, no. 11 (2012): 1406. http://dx.doi.org/10.1039/c2md20096a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Cao, Jiangying, Jie Zang, Chunhua Ma, Xiaoguang Li, Jinning Hou, Jin Li, Yongxue Huang, Wenfang Xu, Binghe Wang, and Yingjie Zhang. "Design, Synthesis, and Biological Evaluation of Pyrazoline-Based Hydroxamic Acid Derivatives as Aminopeptidase N (APN) Inhibitors." ChemMedChem 13, no. 5 (February 16, 2018): 431–36. http://dx.doi.org/10.1002/cmdc.201700690.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Su, Li, Yuping Jia, Lei Zhang, Yingying Xu, Hao Fang, and Wenfang Xu. "Design, synthesis and biological evaluation of novel amino acid ureido derivatives as aminopeptidase N/CD13 inhibitors." Bioorganic & Medicinal Chemistry 20, no. 12 (June 2012): 3807–15. http://dx.doi.org/10.1016/j.bmc.2012.04.035.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Li, Qianbin, Hao Fang, Xuejian Wang, and Wenfang Xu. "Novel cyclic-imide peptidomimetics as aminopeptidase N inhibitors. Structure-based design, chemistry and activity evaluation. II." European Journal of Medicinal Chemistry 45, no. 4 (April 2010): 1618–26. http://dx.doi.org/10.1016/j.ejmech.2009.12.071.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Mahadevan, Daruka, and José W. Saldanha. "The extracellular regions of PSMA and the transferrin receptor contain an aminopeptidase domain: Implications for drug design." Protein Science 8, no. 11 (December 31, 2008): 2546–49. http://dx.doi.org/10.1110/ps.8.11.2546.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Mucha, A., A. Kunert, J. Grembecka, M. Pawełczak, and P. Kafarski. "A phosphonamidate containing aromatic N-terminal amino group as inhibitor of leucine aminopeptidase—design, synthesis and stability." European Journal of Medicinal Chemistry 41, no. 6 (June 2006): 768–72. http://dx.doi.org/10.1016/j.ejmech.2006.03.023.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Wang, Fang, Rong Li, Hui Jian, Zihao Huang, Yingwu Wang, Zheng Guo, and Renjun Gao. "Design and Construction of an Effective Expression System with Aldehyde Tag for Site-Specific Enzyme Immobilization." Catalysts 10, no. 4 (April 8, 2020): 410. http://dx.doi.org/10.3390/catal10040410.

Full text

Abstract:

In recent years, the development and application of site-specific immobilization technology for proteins have undergone significant advances, which avoids the unwanted and random covalent linkage between the support and active site of protein in the covalent immobilization. Formylglycine generating enzyme (FGE) can transform the cysteine from a conversed 6-amino-acid sequence CXPXR into formylglycine with an aldehyde group (also termed as “aldehyde tag”). Based on the frame of pET-28a, the His-tags were replaced with aldehyde tags. Afterward, a set of plasmids were constructed for site-specific covalent immobilization, their His-tags were knock out (DH), or were replaced at different positions: N-terminal (NQ), C-terminal (CQ), or both (DQ) respectively. Three different enzymes, thermophilic acyl aminopeptidase (EC 3.4.19.1) from Sulfolobus tokodaii (ST0779), thermophilic dehalogenase (EC 3.8.1.2) from Sulfolobus tokodaii (ST2570), and Lipase A (EC 3.1.1.3) from Bacillus subtilis (BsLA) were chosen as model enzymes to connect with these plasmid systems. The results showed that different aldehyde-tagged enzymes can be successfully covalently attached to different carriers modified with an amino group, proving the universality of the method. The new immobilized enzyme also presented better thermostability and reutilization than those of the free enzyme.

APA, Harvard, Vancouver, ISO, and other styles

46

Chen, Laizhong, Jiajia Mou, Yingying Xu, Hao Fang, and Wenfang Xu. "Design, synthesis and activity study of aminopeptidase N targeted 3-amino-2-hydroxy-4-phenyl-butanoic acid derivatives." Drug Discoveries & Therapeutics 5, no. 2 (2011): 61–65. http://dx.doi.org/10.5582/ddt.2011.v5.2.61.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

McGowan, S., C. A. Oellig, W. A. Birru, T. T. Caradoc-Davies, C. M. Stack, J. Lowther, T. Skinner-Adams, et al. "Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases." Proceedings of the National Academy of Sciences 107, no. 6 (January 21, 2010): 2449–54. http://dx.doi.org/10.1073/pnas.0911813107.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Zhang, Xiaopan, Jian Zhang, Lei Zhang, Jinghong Feng, Yingying Xu, Yumei Yuan, Hao Fang, and Wenfang Xu. "Design, synthesis and biological evaluation of novel 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid derivatives as aminopeptidase N/CD13 inhibitors." Bioorganic & Medicinal Chemistry 19, no. 20 (October 2011): 6015–25. http://dx.doi.org/10.1016/j.bmc.2011.08.041.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Hernández-Guzmán, K., A. Sahagún-Ruiz, A. J. Vallecillo, I. Cruz-Mendoza, and H. Quiroz-Romero. "Construction and evaluation of a chimeric protein made fromFasciola hepaticaleucine aminopeptidase and cathepsin L1." Journal of Helminthology 90, no. 1 (October 2, 2014): 7–13. http://dx.doi.org/10.1017/s0022149x14000686.

Full text

Abstract:

AbstractLeucine aminopeptidase (LAP) and cathepsin L1 (CL1) are important enzymes for the pathogenesis and physiology ofFasciola hepatica. These enzymes were analysedin silicoto design a chimeric protein containing the most antigenic sequences of LAP (GenBank; AAV59016.1; amino acids 192–281) and CL1 (GenBank CAC12806.1; amino acids 173–309). The cloned 681-bp chimeric fragment (rFhLAP-CL1) contains 270 bp from LAP and 411 bp from CL1, comprising three epitopes, DGRVVHLKY (amino acids 54–62) from LAP, VTGYYTVHSGSEVELKNLV (amino acids 119–137) and YQSQTCLPF (amino acids 161–169) from CL1. The ~25 kDa rFhLAP-CL1 chimeric protein was expressed from the pET15b plasmid in the Rosetta (DE3)Escherichia colistrain. The chimeric protein rFhLAP-CL1, which showed antigenic and immunogenic properties, was recognized in Western blot assays usingF. hepatica-positive bovine sera, and induced strong, specific antibody responses following immunization in rabbits. The newly generated chimeric protein may be used as a diagnostic tool for detection of antibodies againstF. hepaticain bovine sera and as an immunogen to induce protection against bovine fasciolosis.

APA, Harvard, Vancouver, ISO, and other styles

50

Bala, Sandeepchowdary, Kalisha vali Yellamanda, Anilkumar Kadari, Venkata S. U. Ravinuthala, Bhavita Kattula, Om V. Singh, Rambabu Gundla, and Anthony Addlagatta. "Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies." Bioorganic Chemistry 115 (October 2021): 105185. http://dx.doi.org/10.1016/j.bioorg.2021.105185.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!