149204-93-3Relevant articles and documents
Structure-activity study at positions 3 and 4 of human neuropeptide S
Camarda, Valeria,Trapella, Claudio,Calo', Girolamo,Guerrini, Remo,Rizzi, Anna,Ruzza, Chiara,Fiorini, Stella,Marzola, Erika,Reinscheid, Rainer K.,Regoli, Domenico,Salvadori, Severo
, p. 8841 - 8845 (2008)
Neuropeptide S (NPS) has been identified as the endogenous ligand of a previously orphan receptor now named NPSR. Previous studies demonstrated that the N-terminal sequence Phe2-Arg3-Asn4 of the peptide is crucial for biological activity. Here, we report on a focused structure-activity study of Arg3 and Asn4 that have been replaced with a series of coded and non-coded amino acids. Thirty-eight human NPS analogues were synthesized and pharmacologically tested for intracellular calcium mobilization using HEK293 cells stably expressing the mouse NPSR. The results of this study demonstrated the following NPS position 3 structure-activity features: (i) the guanidine moiety and its basic character are not crucial requirements, (ii) an aliphatic amino acid with a linear three carbon atom long side chain is sufficient to bind and fully activate NPSR, (iii) the receptor pocket allocating the position 3 side chain can accommodate slightly larger side chains at least to a certain degree [hArg, Arg(NO2) or Arg(Me)2 but not Arg(Tos)]. Position 4 seems to be more sensitive to amino acids replacement compared to position 3; in fact, all the amino acid replacements investigated produced either an important decrease of biological activity or generated inactive derivatives suggesting a pivotal role of the Asn4 side chain for NPS bioactivity.
A colorimetric sensing ensemble for heparin
Zhong, Zhenlin,Anslyn, Eric V.
, p. 9014 - 9015 (2007/10/03)
A receptor possessing ammoniums and a novel amino acid with a boronic acid side chain was designed and synthesized. The receptor shows good affinity and selectivity for heparin over similar polysaccharides possessing lower anionic charge density. The affi
