Conformation of dynorphin A(1-17) bound to dodecylphosphocholine micelles

Conformation-activity relationships of opioid peptides with selective activities at opioid receptors

“…101,102 Also, the ␣-helical structure from Gly 3 to Arg 9 was found in Dyn A bound to a lipid micelle. 101 Based on these observations, cyclic analogues of Dyn A were synthesized and tested for selectivity for receptor and biological activity.…”

NMR studies of the structure and dynamics of peptide E, an endogenous opioid peptide that binds with high affinity to multiple opioid receptor subtypes

“…9 In contrast to the studies in methanol, a detailed nmr study of dynorphin-A(1-17) in perdeuterated phosphocholine micelles indicated the presence of helical structure in the N-terminal domain spanning residues 3-9. 10 More recent detailed structural analysis demonstrates the existence of a helical domain in the N-terminal region. 11 CD studies of adrenal peptide E have indicated significant helical content in methanolic solution.…”

Metallomicellar Catalysis: Catalytic Cleavage of p-Nitrophenyl Picolinate by Cu2+ Complex of 4-Chloride-2,6-bis(N-hydroxyethylaminomethyl)-benzophenol in Micellar Solution

“…Micelles can concentrate the reactants within their small volumes (1)(2)(3)(4); stabilize substrates, intermediates, or products (5,6); and orient substrates (7)(8)(9) so that ionization potential and oxidation-reduction properties, dissociation constants, physical properties, quantum efficiencies, and reactivity are changed (10)(11)(12). Thus micelles can also alter the reaction rate, mechanism (13), and regio-and stereochemistry (14,15).…”