Modified-amino acid/peptide pyrimidine analogs: Synthesis, structural characterization and DFT study of N-(pyrimidyl) gabapentine and N-(pyrimidyl)baclofen

2021 ◽  
Author(s):  
Angel Garcia-Raso ◽  
ANGEL TERRON ◽  
JUAN J J FIOL ◽  
Adela Lopez-Zafra ◽  
Barbara Massanet ◽  
...  

In this manuscript we report the synthesis and structural characterization of two new pyrimidine amino acid modified derivatives: N-(pyrimidyl)gabapentin (pyr-Gabapentin) (1) and N-(pyrimidyl)baclofen (pyr-baclofen) (2) and the spectroscopic characterization of...

RSC Advances ◽  
2015 ◽  
Vol 5 (12) ◽  
pp. 9010-9018 ◽  
Author(s):  
Lorenzo Biancalana ◽  
Marco Bortoluzzi ◽  
Claudia Forte ◽  
Fabio Marchetti ◽  
Guido Pampaloni

A joint spectroscopic and computational study has allowed us to determine the dinuclear structural core of the products of the reactions between molybdates and α-amino acids in aqueous medium.


2021 ◽  
Vol 1224 ◽  
pp. 129022
Author(s):  
Zhang Ying ◽  
Naren Gerile ◽  
Hua Er ◽  
Zhang Jinkang ◽  
Shi Yifeng

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.


1997 ◽  
Vol 543 (1-2) ◽  
pp. 135-143 ◽  
Author(s):  
Pradeep Mathur ◽  
Aswini K. Dash ◽  
Md. Munkir Hossain ◽  
C.V.V. Satyanarayana ◽  
Arnold L. Rheingold ◽  
...  

2010 ◽  
Vol 6 (8) ◽  
pp. e1001034 ◽  
Author(s):  
Shinya Yamada ◽  
Masato Hatta ◽  
Bart L. Staker ◽  
Shinji Watanabe ◽  
Masaki Imai ◽  
...  

Toxicon ◽  
2012 ◽  
Vol 60 (7) ◽  
pp. 1263-1276 ◽  
Author(s):  
Cristiane Bregge-Silva ◽  
Maria Cristina Nonato ◽  
Sérgio de Albuquerque ◽  
Paulo Lee Ho ◽  
Inácio L.M. Junqueira de Azevedo ◽  
...  

2002 ◽  
Vol 68 (8) ◽  
pp. 3830-3840 ◽  
Author(s):  
Shinichi Kawamoto ◽  
Jun Shima ◽  
Rumi Sato ◽  
Tomoko Eguchi ◽  
Sadahiro Ohmomo ◽  
...  

ABSTRACT Mundticin KS, a bacteriocin produced by Enterococcus mundtii NFRI 7393 isolated from grass silage in Thailand, is active against closely related lactic acid bacteria and the food-borne pathogen Listeria monocytogenes. In this study, biochemical and genetic characterization of mundticin KS was done. Mundticin KS was purified to homogeneity by ammonium sulfate precipitation, sequential ion-exchange chromatography, and solid-phase extraction. The gene cluster (mun locus) for mundticin KS production was cloned, and DNA sequencing revealed that the mun locus consists of three genes, designated munA, munB, and munC. The munA gene encodes a 58-amino-acid mundticin KS precursor, munB encodes a protein of 674 amino acids involved in translocation and processing of the bacteriocin, and munC encodes a mundticin KS immunity protein of 98 amino acids. Amino acid and nucleotide sequencing revealed the complete, unambiguous primary structure of mundticin KS; mundticin KS comprises a 43-amino-acid peptide with an amino acid sequence similar to that of mundticin ATO6 produced by E. mundtii ATO6. Mundticin KS and mundticin ATO6 are distinguished by the inversion of the last two amino acids at their respective C termini. These two mundticins were expressed in Escherichia coli as recombinant peptides and found to be different in activity against certain Lactobacillus strains, such as Lactobacillus plantarum and Lactobacillus curvatus. Mundticin KS was successfully expressed by transformation with the recombinant plasmid containing the mun locus in heterogeneous hosts such as E. faecium, L. curvatus, and Lactococcus lactis. Based on our results, the mun locus is located on a 50-kb plasmid, pML1, of E. mundtii NFRI 7393.


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