Pharmacology of a new tritiated endomorphin-2 analog containing the proline mimetic cis-2-aminocyclohexanecarboxylic acid.

As part of ongoing work aimed at generating proteolytically stable, readily applicable, radiolabeled endomorphin-2 (EM-2) analogs for elucidation of the topological requirements of peptide binding to μ-opioid receptors, we report here on the synthesis, radiolabeling, binding kinetics and binding site distribution of an EM-2 analog in which Pro(2) is replaced by 2-aminocyclohexanecarboxylic acid, ACHC. [(3)H][(1S,2R)ACHC](2)EM-2 (specific activity 63.49Ci × mmol(-1)) bound specifically to its binding sites with high affinity (K(D) = 0.

Thermodynamics of micelle formation of the counterion coupled gemini surfactant Bis(4-(2-dodecyl)benzenesulfonate)-Jeffamine salt and its dynamic adsorption on sandstone.

A novel counterion-coupled gemini (cocogem) surfactant, DBSJ, was synthetized via the 2:1 coupling reaction between 4-(2-dodecyl)benzenesulfonic acid (Lutensit A-LBS) and polypropyleneglycol-bis(2-aminopropyl) ether (Jeffamine D230). The surfactant had a polydispersity index of Mw/Mn = 1.04, as determined by electrospray-ionization mass spectrometry.

New endomorphin analogues containing alicyclic beta-amino acids: influence on bioactive conformation and pharmacological profile.

Endomorphins were subjected to a number of structural modifications in a search for their bioactive conformations. The alicyclic beta-amino acids cis-(1 S,2 R)ACPC/ACHC, cis-(1 R,2 S)ACPC/ACHC, trans-(1 S,2 S)ACPC/ACHC, and trans-(1 R,2 R)ACPC/ACHC were introduced into endomorphins to examine the conformational effects on the bioactivity. Use of a combination of receptor binding techniques, (1)H NMR, and molecular modeling allowed the conclusion that Pro (2) substitution by these residues causes changes in structure, proteolytic stability, and pharmacological activity.