51847-39-3Relevant articles and documents
Backbone modification of retinal induces protein-like excited state dynamics in solution
Sovdat, Tina,Bassolino, Giovanni,Liebel, Matz,Schnedermann, Christoph,Fletcher, Stephen P.,Kukura, Philipp
supporting information; experimental part, p. 8318 - 8320 (2012/06/30)
The drastically different reactivity of the retinal chromophore in solution compared to the protein environment is poorly understood. Here, we show that the addition of a methyl group to the C=C backbone of all-trans retinal protonated Schiff base acceler
Cyclodextrin retinylidene: A biomimetic kinetic trap model for rhodopsin
Kpegba, Kafui,Murtha, Matthew,Nesnas, Nasri
, p. 1523 - 1526 (2007/10/03)
All trans retinal was attached to both the primary face and the secondary face of β-cyclodextrin via a Schiff base linkage, analogous to that in rhodopsin. The new models were evaluated and compared with n-butylamine retinylidene Schiff base for their rates of hydrolysis, and factors that influence such rates. Competition studies using adamantane carboxylate demonstrated the kinetic trap theory by diminishing the binding of retinal in the cyclodextrin, thereby augmenting the rate of hydrolysis. NMR experiments indicate that the retinylidene is most probably bound in the form of a dimer.
Liposome stabilised retinal Schiff bases
Das, Joydip,Singh, Anil K.
, p. 615 - 617 (2007/10/02)
All-trans-N-retinylidene-n-butylamine (3) can be stabilised in liposomes of phosphatidylcholine.The rate of romation of the Schiff base is found to decrease with increasing chloesterol concentration in the membrane.