Bicyclic tetrapeptides as potent HDAC inhibitors: effect of aliphatic loop position and hydrophobicity on inhibitory activity.
Several histone deacetylase (HDAC) inhibiting bicyclic tetrapeptides have been designed and synthesized through intramolecular ring-closing metathesis (RCM) reaction and peptide cyclization. We designed bicyclic tetrapeptides based on CHAP31, trapoxin B and HC-toxin I. The HDAC inhibitory and p21 promoter assay results showed that the aliphatic loop position as well as the hydrophobicity plays an important role toward the activity of the bicyclic tetrapeptide HDAC inhibitors.
['Islam|Md Nurul|MN|', 'Islam|Md Shahidul|MS|', 'Hoque|Md Ashraful|MA|', 'Kato|Tamaki|T|', 'Nishino|Norikazu|N|', 'Ito|Akihiro|A|', 'Yoshida|Minoru|M|']
D056572:Histone Deacetylase Inhibitors D006655:Histone Deacetylases D006801:Humans D057927:Hydrophobic and Hydrophilic Interactions D036341:Intercellular Signaling Peptides and Proteins D009842:Oligopeptides D010455:Peptides D010456:Peptides, Cyclic D011485:Protein Binding
Bicyclic tetrapeptides Aliphatic loop position Ring-closing metathesis Histone deacetylase inhibitors