Anil Kumar Marapaka

Anil Kumar Marapaka
  • Doctor of Philosophy
  • PostDoc Position at Purdue University West Lafayette

About

17
Publications
4,618
Reads
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239
Citations
Current institution
Purdue University West Lafayette
Current position
  • PostDoc Position
Additional affiliations
April 2019 - present
Purdue University West Lafayette
Position
  • PostDoc Position
October 2014 - present
Indian Institute of Chemical Technology
Position
  • CSIR-SRF
October 2011 - September 2014
Indian Institute of Chemical Technology
Position
  • Project Assistant
Education
October 2014 - December 2018
Indian Institute of Chemical Technology
Field of study
  • Structural Biology

Publications

Publications (17)
Article
Full-text available
Studies on Metal nanoparticles synthesized using plant extracts are drawing much attention in the research studies due to their distinctive physicochemical, electrical and magnetic properties. As these Plant Extracts contain polyphenols, flavonoids, ions, etc which help in the formation of the good nanoparticles with better yields. The nanoparticle...
Article
Full-text available
Carbonic anhydrases (CAs) from the pathogenic bacteria Nesseria gonorrhoeae and vancomycin-resistant enterococci (VRE) have recently been validated as antibacterial drug targets. Here we explored the inhibition of the α-CA from N. gonorrhoeae (α-NgCA), of α- and γ-class enzymes from Enterococcus faecium (α-EfCA and γ-EfCA) with a panel of aliphatic...
Article
Drug-resistant Neisseria gonorrhoeae is a critical threat to public health, and bacterial carbonic anhydrases expressed by N. gonorrhoeae are potential new therapeutic targets to combat this pathogen. To further expand upon our recent reports of bacterial carbonic anhydrase inhibitors for the treatment of N. gonorrhoeae, our team has solved ligand-...
Article
Full-text available
Plasmodium parasites causing malaria have developed resistance to most of the antimalarials in use, including the artemisinin-based combinations, which are the last line of defense against malaria. This necessitates the discovery of new targets and the development of novel antimalarials. Plasmodium falciparum alanyl aminopeptidase (PfA-M1) and leuc...
Article
Neisseria gonorrhoeae is an urgent threat to public health in the United States and around the world. Many of the current classes of antibiotics to treat N. gonorrhoeae infection are quickly becoming obsolete due to increased rates of resistance. Thus, there is a critical need for alternative antimicrobial targets and new chemical entities. Our tea...
Article
Puromycin sensitive aminopeptidase (PSA or NPEPPS) is a M1 class aminopeptidase is selectively inhibited by the natural product puromycin, an aminonucleoside antibiotic produced by the bacterium Streptomyces alboniger. The molecular basis for this selective inhibition has not been understood well. Here, we report the basis for selectivity of puromy...
Article
Full-text available
In the present study some new isoaxazole based Shciff base binary metal complexes were synthesized from Schiff base ligand The spectral studies revealed that Co(II) and Cu(II) complexes have octahedral geometry; Zn(II) complex has Tetrahedral structure where as Pd(II) complex shown square planar geometry. The Schiff base ligand and its correspondin...
Article
Natural product ovalicin and its synthetic derivative TNP-470 have been extensively studied for their anti-angiogenic property, and the later reached phase 3 clinical trials. They covalently modify the conserved histidine in Type 2 methionine aminopeptidases (MetAPs) at nanomolar concentrations. Even though a similar mechanism is possible in Type 1...
Article
Methionine aminopeptidases (MetAPs) are a class of enzymes evolved to cleave initiator methionine in 60–70% of the total cellular proteins in all living cells. Based on their sequence differences, they are classified into Type 1 and Type 2. Type 1 is further divided into Type 1a, 1a′, 1b, 1c and 1d. Irrespective of various classifications, all MetA...
Article
Full-text available
The synthesis of racemic substituted 7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochlorides was optimized to enhance reproducibility and increase the overall yield. In order to investigate their specificity, series of enzyme inhibition assays were carried out against a diversity of proteases, covering representative members of aspartic, cy...
Article
Aminopeptidases catalyze the hydrolysis of amino acids from the N-terminus of protein or peptide substrates. M1 family aminopeptidases are important for the pathogenicity of bacteria and play critical role in many physiological processes such as protein maturation, regulation of peptide hormone levels in humans. Most of the M1 family aminopeptidase...
Article
Full-text available
In the present study, green synthesis of bimetallic silver and copper nanoparticles were carried out using fruit pulp of Palmyra and characterized using UV-visible spectra, Fourier transform infrared spectra, Scanning electron microscopy and Raman spectroscopy. To investigate if fruit pulp can be used for simultaneous synthesis of two different nan...
Article
Full-text available
Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the major differences in terms of substrate binding pockets between these families is presence (in M1 aminop...
Article
Full-text available
Methionine aminopeptidases (MetAPs) are essential enzymes that make them good drug targets in cancer and microbial infections. MetAPs remove the initiator methionine from newly synthesized peptides in every living cell. MetAPs are broadly divided into Type I and Type II classes. Both prokaryotes and eukaryotes contain Type I MetAPs while eukaryotes...

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