A newly designed key-hole button.

Patients who have undergone frontotemporal craniotomy occasionally complain of scalp deformity in the anterior temporal area. This occurs as a result of inappropriate reconstruction of the temporal muscle and repair of the bone defect at the key hole and surrounding skull. Although several methods have been developed to prevent skin indentation on burr holes located over the convexity, satisfactory cosmetic repair of the key hole remains difficult because of its complicated bone curvature. To prevent such postoperative deformity, the authors designed a button made of hydroxyapatite ceramics to fit the key hole easily. This new, biocompatible "key-hole button" is shaped to alleviate the deformity of the temple by filling the bone defect in a more natural way. The specifications of this device and its clinical application are described.

Solution conformation of mu-selective dermorphin and delta-selective deltorphin-I in phospholipid micelles, studied by NMR spectroscopy and molecular dynamics simulations.

Complete proton resonance assignments of the naturally occurring mu-selective dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) and delta-selective deltorphin-I (H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) were carried out by two-dimensional 1H-NMR techniques to investigate the conformational features in the membrane-mimetic micelles of perdeuterated dodecylphosphocholine. Fifty possible three-dimensional structures for respective peptides were generated by means of distance geometry calculations, all of which satisfy the proton-proton distances derived from NOE measurements within the allowable range, and 25 of them were subjected to the molecular dynamics simulations for 10 ps, in which the NOE distances were included as the energetic constraints. Although conformers simulated for dermorphin showed relatively large conformational variations because of the limited NOE data, most of them were characterized as an entirely folded structure bent at the Gly4 residue, where each of the N- and C-terminal tetrapeptides took an extended conformation. On the other hand, most conformations of deltorphin-I showed the common feature that the N-terminal Tyr-D-Ala-Phe-Asp and C-terminal Val-Val-Gly-NH2 sequences took respective folded conformations, and these were almost at right angles on the border of the Asp-Val sequence. These conformational characteristics are discussed in terms of the possible relationship with the mu/delta-opioid receptor selectivity.