2776-60-5Relevant articles and documents
Enhanced Mechanical and Helical Properties with Achiral Calix[4]arene in a Co-Assembled Hydrogel with a Helical Structure
Choi, Heekyoung,Seo, Hyowon,Go, Misun,Lee, Shim Sung,Jung, Jong Hwa
, p. 219 - 222 (2018)
A mixture of the building blocks 1A and 2G, featuring d-alanine moieties and glycine-functionalized calix[4]arene moieties, respectively, formed a co-assembled hydrogel. In particular, the remarkable enhancement of helical intensity of co-assembled gel was controlled by achiral calix[4]arene 2G, which was attributed to the bridging effect between 1A and 2G, similar to a helical structure. Furthermore, the improvement of the mechanical strength (G′ and G′′ values) of the co-assembled hydrogel prepared with 1.0 equivalent of 2G were around 7000 % and 4400 % stronger, respectively, compared to the gel prepared from the 0.25 equivalents of 2G. The improved mechanical strength was attributed to the formation of a network structure with a H-bonding interaction between 1A and 2G. The results indicate that the enhanced helical and mechanical strength of the co-assembled gel could be controlled by achiral component 2G.
Mitochondria-targeting oxidovanadium(IV) complex as a near-ir light photocytotoxic agent
Prasad, Puja,Khan, Imran,Kondaiah, Paturu,Chakravarty, Akhil R.
, p. 17445 - 17455 (2013)
Oxidovanadium(IV) complexes [VO(L1)(phen)]×Cl (1) and [VO(L2)(L3)]×Cl (2), in which HL1 is 2-{[(benzimidazol-2-yl)methylimino]-methyl}phenol (sal-ambmz), HL2 is 2-[({1-[(anthracen-9-yl)methyl]-benzimi
The discovery of allyltyrosine based tripeptides as selective inhibitors of the HIV-1 integrase strand-transfer reaction
Dalton, Neal,Gordon, Christopher P.,Boyle, Timothy P.,Vandegraaf, Nicholas,Deadman, John,Rhodes, David I.,Coates, Jonathan A.,Pyne, Stephen G.,Keller, Paul A.,Bremner, John B.
supporting information, p. 6010 - 6023 (2016/07/06)
From library screening of synthetic antimicrobial peptides, an O-allyltyrosine-based tripeptide was identified to possess inhibitory activity against HIV-1 integrase (IN) exhibiting an IC50 value of 17.5 μM in a combination 3′-processing and strand transfer microtitre plate assay. The tripeptide was subjected to structure-activity relationship (SAR) studies with 28 peptides, incorporating an array of natural and non-natural amino acids. Resulting SAR analysis revealed the allyltyrosine residue was a key feature for IN inhibitory activity whilst incorporation of a lysine residue and extended hydrophilic chains bearing a terminal methyl ester was advantageous. Addition of hydrophobic aromatic moieties to the N-terminal of the scaffold afforded compounds with improved inhibitory activity. Consolidation of these functionalities lead to the development of the tripeptide 96 which specifically inhibited the IN strand-transfer reaction with an IC50 value of 2.5 μM.
