Synthesis and structure of 6-substituted 9-(2-ethoxy-1,3-dioxan-5-yl)purines

Mishnev, A. F.; Bleidelis, Ya. Ya.; Лиепиньш, Э. Э.; Ramzaeva, N.; Goncharova, I. N.

doi:10.1007/bf00473568

Cited by 4 publications

(3 citation statements)

References 17 publications

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“…Interestingly, other applications of ureidopeptides to biology include the synthesis of Leu-enkephalin analogues [ 36 ], gastrin antagonists [ 37 ] protease inhibitors [ 38 ] and a growth hormone with strong in vivo activity in the rats [ 39 ]. However, little is known about the conformational preferences of pseudopeptides incorporating one or several ureido units [ 40 , 41 ].…”

Section: The Peptide Bond As An Immunotherapeutic Target For Molecmentioning

confidence: 99%

“…Guichard and coworkers started to investigate the intra-molecular H-bonding propensities and conformational behavior of model ureidopeptides in solution [ 41 ]. As a result of competitive conjugation, the rotation barriers of substituted ureas are lower than those of its corresponding native amides, and one might expect greater flexibility of the urea linkage in solution.…”

Section: The Peptide Bond As An Immunotherapeutic Target For Molecmentioning

confidence: 99%

“…Accordingly, we found that the urea moiety in simple N -acyl- N -carbamoyl- gem -diaminolalkyl residues bearing proteinogenic side-chains adopts a cis , trans ( E , Z ) geometry that can be further stabilized by an intra-molecular H-bond in a non-polar organic solvent. The resulting eight-membered (C8) H-bonded ring has been termed a “urea turn” [ 41 ]. With the aim to study in more detail the propensity for urea turn formation in a more comprehensive set of ureidopeptides, including previously unreported oligo-urea/peptide hybrids (made of alternating urea and amide moieties), as well as to incorporate ureido moieties into bioactive peptide segments [ 42 ], the group of Guichard have investigated the preparation and reactivity of a variety of succinimidyl carbamates derived from N -protected α-amino acids and dipeptides.…”

Section: The Peptide Bond As An Immunotherapeutic Target For Molecmentioning

confidence: 99%

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Development of Designed Site-Directed Pseudopeptide-Peptido-Mimetic Immunogens as Novel Minimal Subunit-Vaccine Candidates for Malaria

et al. 2010

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Synthetic vaccines constitute the most promising tools for controlling and preventing infectious diseases. When synthetic immunogens are designed from the pathogen native sequences, these are normally poorly immunogenic and do not induce protection, as demonstrated in our research. After attempting many synthetic strategies for improving the immunogenicity properties of these sequences, the approach consisting of identifying high binding motifs present in those, and then performing specific changes on amino-acids belonging to such motifs, has proven to be a workable strategy. In addition, other strategies consisting of chemically introducing non-natural constraints to the backbone topology of the molecule and modifying the α-carbon asymmetry are becoming valuable tools to be considered in this pursuit. Non-natural structural constraints to the peptide backbone can be achieved by introducing peptide bond isosters such as reduced amides, partially retro or retro-inverso modifications or even including urea motifs. The second can be obtained by strategically replacing L-amino-acids with their enantiomeric forms for obtaining both structurally site-directed designed immunogens as potential vaccine candidates and their Ig structural molecular images, both having immuno-therapeutic effects for preventing and controlling malaria.

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