tetano
Editor, Senior Moderator
J Med Chem. 2014 Sep 24. [Epub ahead of print]
Synthesis and influenza virus inhibitory activities of carbosilane dendrimers peripherally-functionalized with hemagglutinin-binding peptide.
Hatano K, Matsubara T, MUramatsu Y, Ezure1 M, Koyama T, Matsuoka K, Kuriyama R, Kori H, Sato T.
Abstract
A series of carbosilane dendrimers uniformly functionalized with hemagglutinin (HA)-binding peptide (sialic acid-mimic peptide; Ala-Arg-Leu-Pro-Arg) was systematically synthesized and their anti-influenza virus activity was evaluated. The carbosilane-based peptide dendrimers, unlike sialylated dendrimers, cannot be digested by virus neuraminidases. The peptide dendrimers exhibited intriguing biological activities depending on the form of their core frame, with a dumbbell-type peptide dendrimer showing particularly strong inhibitory activities against two human influenza viruses, A/PR/8/34 (H1N1) and A/Aichi/2/68 (H3N2). The IC50 values of the dumbbell-type peptide dendrimer for both strains were 0.1 ?M, the highest activity among the HA-binding peptide derivatives. The results suggest that a dumbbell-shaped carbosilane dendrimer is the most suitable core scaffold for HA-binding peptide dendrimers.
PMID:
25249262
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25249262
Synthesis and influenza virus inhibitory activities of carbosilane dendrimers peripherally-functionalized with hemagglutinin-binding peptide.
Hatano K, Matsubara T, MUramatsu Y, Ezure1 M, Koyama T, Matsuoka K, Kuriyama R, Kori H, Sato T.
Abstract
A series of carbosilane dendrimers uniformly functionalized with hemagglutinin (HA)-binding peptide (sialic acid-mimic peptide; Ala-Arg-Leu-Pro-Arg) was systematically synthesized and their anti-influenza virus activity was evaluated. The carbosilane-based peptide dendrimers, unlike sialylated dendrimers, cannot be digested by virus neuraminidases. The peptide dendrimers exhibited intriguing biological activities depending on the form of their core frame, with a dumbbell-type peptide dendrimer showing particularly strong inhibitory activities against two human influenza viruses, A/PR/8/34 (H1N1) and A/Aichi/2/68 (H3N2). The IC50 values of the dumbbell-type peptide dendrimer for both strains were 0.1 ?M, the highest activity among the HA-binding peptide derivatives. The results suggest that a dumbbell-shaped carbosilane dendrimer is the most suitable core scaffold for HA-binding peptide dendrimers.
PMID:
25249262
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25249262