ChemInform Abstract: Design and Synthesis of Conformationally Constrained Arginal Thrombin Inhibitors.

Salimbeni, A.; Paleari, F.; Canevotti, Renato; Criscuoli, Marco; Lippi, Annalisa; Angiolini, Mauro; Belvisi, Laura; Scolastico, Carlo; Colombo, Lino

doi:10.1002/chin.199801221

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“…Detailed conformational analysis by nuclear magnetic resonance, infrared, and molecular modeling techniques [67], as well as applications as thrombin inhibitors [68], and in RGD-based cyclopeptides such as a v b 3 -integrin ligands [69], proved this class of compounds to act as d-amino acid reverse turn mimetics.…”

Section: D-amino Acids As Reverse Turn Mimeticsmentioning

confidence: 99%

Synthesis of γ‐ and δ‐Amino Acids

Trabocchi

Menchi

Guarna

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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An area of significant importance that provides new dimensions to the field of molecular diversity and drug discovery is the area of peptidomimetics [1]. Biomedical research has reoriented towards the development of new drugs based on peptides and proteins, by introducing both structural and functional specific modifications, and maintaining the features responsible for biological activity. As a part of this research area, unnatural amino acids are of valuable interest in drug discovery and their use as new building blocks for the development of peptidomimetics with a high structural diversity level is of key interest. In particular, medicinal chemistry has taken advantage of the use of amino acid homologs to introduce elements of diversity for the generation of new molecules as drug candidates in the so-called peptidomimetic approach, where a peptide lead is processed into a new nonpeptidic molecule. The additional methylenic unit between the N-and C-termini in b-amino acids results in an increase of the molecular diversity in terms of the higher number of stereoisomers and functional group variety, and many synthetic approaches to the creation of b-amino acids have been published. There is great interest in these as a tool for medicinal chemistry [2] and in the field of b-peptides generally [3]. The g-and d-amino acids have garnered similar interest. In particular, the folding properties of g-[4] and d-peptides [5] have been investigated, as they have been proved to generate stable secondary structures. The homologation of a-amino acids into g-and d-units allows an enormous increase of the chemical diversity within the three and four atoms between the amino and carboxyl groups. Thus, additional substituents and stereocenters expand the number of compounds belonging to the class of g-and d-amino acids. g-Amino acids have been reported both in linear form, and with the amino and carboxyl groups separated or incorporated in a cyclic structure. In the case of d-amino acids, five-and six-membered rings have been mainly reported having two substituents variously tethered between the amino and carboxyl groups. Moreover, bicyclic and spiro compounds have been reported as constrained d-amino acids, especially in the field of peptidomimetics. The synthetic approaches for the preparation of

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Section: D-amino Acids As Reverse Turn Mimeticsmentioning

confidence: 99%