			Home About us Contact

Surface Recognition (surface + recognition)

Distribution by Scientific Domains

Chemistry	50%

Selected Abstracts

Controlled Assembly of Protein,Nanoparticle Composites through Protein Surface Recognition,

ADVANCED MATERIALS, Issue 5 2005
S. Srivastava
Controlled assembly of protein,nanoparticle composites through complementary protein surface recognition is demonstrated. Interaction of an unstable protein (chymotrypsin) with a gold nanoparticle results in close interparticle spacing, while a stable protein (cytochrome,C) that retains its structure upon binding produces a hybrid material with a larger interparticle distance (see Figure). [source]

The role of side chain conformational flexibility in surface recognition by Tenebrio molitor antifreeze protein

PROTEIN SCIENCE, Issue 7 2003
Margaret E. Daley
AFP, antifreeze protein; DQF-COSY, double quantum filtered correlated spectroscopy; NMR, nuclear magnetic resonance; NOE, nuclear Overhauser enhancement; NOESY, nuclear Overhauser effect spectroscopy; 3J,,, 3-bond scalar coupling constant between spins H, and H, Abstract Two-dimensional nuclear magnetic resonance spectroscopy was used to investigate the flexibility of the threonine side chains in the ,-helical Tenebrio molitor antifreeze protein (TmAFP) at low temperatures. From measurement of the 3J,,1H- 1H scalar coupling constants, the ,1 angles and preferred rotamer populations can be calculated. It was determined that the threonines on the ice-binding face of the protein adopt a preferred rotameric conformation at near freezing temperatures, whereas the threonines not on the ice-binding face sample many rotameric states. This suggests that TmAFP maintains a preformed ice-binding conformation in solution, wherein the rigid array of threonines that form the AFP-ice interface matches the ice crystal lattice. A key factor in binding to the ice surface and inhibition of ice crystal growth appears to be the close surface-to-surface complementarity between the AFP and crystalline ice, and the lack of an entropic penalty associated with freezing out motions in a flexible ligand. [source]

Synthesis of N -Hydroxycinnamides Capped with a Naturally Occurring Moiety as Inhibitors of Histone Deacetylase

CHEMMEDCHEM, Issue 4 2010
Wei-Jan Huang Prof.
Abstract Histone deacetylase (HDAC) inhibitors are regarded as promising therapeutics for the treatment of cancer. All reported HDAC inhibitors contain three pharmacophoric features: a zinc-chelating group, a hydrophobic linker, and a hydrophobic cap for surface recognition. In this study we investigated the effectiveness of osthole, a hydrophobic Chinese herbal compound, as the surface recognition cap in hydroxamate-based compounds as inhibitors of HDAC. Nine novel osthole-based N -hydroxycinnamides were synthesized and screened for enzyme inhibition activity. Compounds 9,d, 9,e, 9,g exhibited inhibitory activities (IC50=24.5, 20.0, 19.6,nM) against nuclear HDACs in HeLa cells comparable to that of suberoylanilide hydroxamic acid (SAHA; IC50=24.5,nM), a potent inhibitor clinically used for the treatment of cutaneous T-cell lymphoma (CTCL). While compounds 9,d and 9,e showed SAHA-like activity towards HDAC1 and HDAC6, compound 9,g was more selective for HDAC1. Compound 9,d exhibited the best cellular effect, which was comparable to that of SAHA, of enhancing acetylation of either ,-tubulin or histone H3. Molecular docking analysis showed that the osthole moiety of compound 9,d may interact with the same hydrophobic surface pocket exploited by SAHA and it may be modified to provide class-specific selectivity. These results suggest that osthole is an effective hydrophobic cap when incorporated into N -hydroxycinnamide-derived HDAC inhibitors. [source]