Sanderson, John M. (2007) 'Refined models for the preferential interactions of tryptophan with phosphocholines.', Organic & biomolecular chemistry., 5 (20). pp. 3276-3286.
A series of molecular models of the adducts formed between N-acetyl-L-tryptophan ethylamide and diacetyl-sn-glycero-3-phosphocholine have been generated. Using rOesy data that enabled us to place restrictions on the proximity of a number of key protons in the amino acid/phosphocholine pairs, a series of structures were generated following molecular dynamics and mechanics experiments using the CHARMM27 force field. These structures were then subjected to a series of clustering algorithms in order to classify the tight binding interactions between a single tryptophan and a phosphocholine. From these analyses, it is evident that: (i) binding is characterised by hydrogen bonding between the indole NH as donor and phosphate oxygen as acceptor, cation–carbonyl interactions between the choline ammonium and amide carbonyl groups and cation– interactions; (ii) cation– interactions are not always observed, particularly when their formation is at the expense of cation–carbonyl and hydrogen bonding interactions; (iii) on the basis of amino acid torsional parameters, it is possible to predict whether the phosphocholine headgroup will bind in a compact or elongated conformation. Extension of the procedures to characterise 2 : 1 Trp–PC binding revealed that the same intermolecular interactions are predominant; however, combinations of all three intermolecular interactions within the same adduct occur much more frequently due to the availability of donor/acceptor groups from both tryptophans in the 2 : 1 system.
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|Publisher Web site:||http://dx.doi.org/10.1039/b707502b|
|Record Created:||21 Jun 2011 10:35|
|Last Modified:||21 Jun 2011 13:17|
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