Retropubic, laparoscopic and mini-laparoscopic radical prostatectomy : a prospective assessment of patient scar satisfaction

Published online: 26 October 2014PURPOSE: To compare patient scar satisfaction after retropubic, standard laparoscopic, mini-laparoscopic (ML) and open radical prostatectomy (RP). METHODS: Patients undergoing RP for a diagnosis of localized prostate cancer at a single academic hospital between September 2012 and December 2013 were enrolled in this prospective nonrandomized study. The patients were included in three study arms: open surgery, VLP and ML. A skin stapler was used for surgical wound closure in all cases. Demographic and main surgical outcomes, including perioperative complications, were analyzed. Surgical scar satisfaction was measured using the Patient and Observer Scar Assessment Questionnaire (POSAS) and the two Body Image Questionnaire (BIQ) scales, respectively, recorded at skin clips removal and either at 6 months after surgery. RESULTS: Overall, 32 patients were enrolled and completed the 6 month of follow-up. At clips removal, laparoscopic approaches offered better scar result than open surgery according to the POSAS. However, at 6 months, no differences were detected between VLP and open, whereas ML was still associated with a better scar outcome (p = 0.001). This finding was also confirmed by both BIQ scales, including the body image score (ML 9.8 ± 1.69, open 15.73 ± 3.47, VLP 13.27 ± 3.64; p = 0.001) and the cosmetic score (ML 16.6 ± 4.12, open 10 ± 1.9, LP 12.91 ± 3.59; p = 0.001). Small sample size and lack of randomization represent the main limitations of this study. CONCLUSIONS: ML RP offers a better cosmetic outcome when compared to both open and standard laparoscopic RP, representing a step toward minimal surgical scar. The impact of scar outcome on RP patients' quality of life remains to be determined

Clinical Pharmacokinetics and Dose Recommendations for Posaconazole in Infants and Children.

OBJECTIVES: The objectives of this study were to investigate the population pharmacokinetics of posaconazole in immunocompromised children, evaluate the influence of patient characteristics on posaconazole exposure and perform simulations to recommend optimal starting doses. METHODS: Posaconazole plasma concentrations from paediatric patients undergoing therapeutic drug monitoring were extracted from a tertiary paediatric hospital database. These were merged with covariates collected from electronic sources and case-note reviews. An allometrically scaled population-pharmacokinetic model was developed to investigate the effect of tablet and suspension relative bioavailability, nonlinear bioavailability of suspension, followed by a step-wise covariate model building exercise to identify other important sources of variability. RESULTS: A total of 338 posaconazole plasma concentrations samples were taken from 117 children aged 5 months to 18 years. A one-compartment model was used, with tablet apparent clearance standardised to a 70-kg individual of 15 L/h. Suspension was found to have decreasing bioavailability with increasing dose; the estimated suspension dose to yield half the tablet bioavailability was 99 mg/m2. Diarrhoea and proton pump inhibitors were also associated with reduced suspension bioavailability. CONCLUSIONS: In the largest population-pharmacokinetic study to date in children, we have found similar covariate effects to those seen in adults, but low bioavailability of suspension in patients with diarrhoea or those taking concurrent proton pump inhibitors, which may in particular limit the use of posaconazole in these patients

CRYSTAL-STRUCTURES OF A D-RESIDUE CONTAINING TETRAPEPTIDES .1. TERT-BOC-D-VALYL-ALANYL-LEUCYL-ALANYL METHOXIDE, BUTANOL SOLVATE

The crystal structure of a heterochiral peptide, viz. Boc-D-Val-Ala-Leu-Ala-OMe, with a D-residue in the beginning of the sequence has been determined (a = 9.464(5), b = 35.615(5), c = 9.703(2) Angstrom, space group P2(1)2(1)2, Z = 4, R = 0.09). The peptide is in the extended beta-conformation and the packing is stabilised by four N-H...O hydrogen bonds in an antiparallel beta-sheet arrangement. The solvent molecule is disordered and does not have any specific interactions with the peptide. (C) Munksgaard 1995

HARNESSING D-AMINO ACIDS FOR PEPTIDE MOTIF DESIGNS - SYNTHESIS AND SOLUTION CONFORMATION OF BOC-D-GLU-ALA-GLY-LYS-NHME AND BOC-L-GLU-ALA-GLY-LYS-NHME

In examining the use of D-amino acids in designing specific peptide folding motifs, the tetrapeptide Boc-D-Glu-Ala-Gly-Lys-NHMe 1 and its analog 2 featuring L-Glu were synthesized for a comparison of their solution conformations by NMR spectroscopy. The temperature coefficients of amide proton resonances, NOE data, side-chain CH2 anisotropies and salt titration results suggest a weak type II reverse-turn conformation for peptide 2, and a tandem type II' turn-3(10)-helix conformation of appreciable conformational stability for peptide I in apolar solvents. The latter is of potential interest as the N-terminal helix cap that could support the design of longer 3(10) helices. Possible origins of appreciable difference in the conformational stabilities of the diastereomers are discussed. (C) Munksgaard 1994

Variation pattern and ecology of plantago Lanceolata Linn.

The study based on variation pattern and ecology of Lanceolata linn supported with transplant experiment reveales that the erect or prostate habit and the pubesence of the leaves are the only two variable characters that are retained if such plants are grown side by side under the uniform conditions of growth. The study recognized four eco types: 1. Plants with erect and smooth and erect scapes (`Es'type); 2. Plants with hairy and erect leaves (`Eh'type); 3. Plants with prostate and smooth leaves and decumbent shape (`ps type) 4. Plants with prostate and smooth leaves and document scape (`ph type). A Comparative ecological study of these four types reveals that these differ from one another in number of fruit/spike, fruit output/plant, fruit dimension, length of the spike, seeds etc. Besides,comparative account of the germination behavior of both fresh and harvested seeds as well as pre-stored seeds collected from four types of species are given in the study

STABLE TYPE-II REVERSE TURN - 3(10) HELIX CONFORMATION OF BOC-D-GLU-ALA-GLY-LYS-ALA-LEU-OME IN APOLAR SOLVENTS

The solution conformation of the title compound, based on one and two dimensional NMR techniques in CDCl3 and (CD3)2SO at 500 MHz, has been deduced as a 310 helix initiated by an electrostatically locked type II' reverse turn

Simulated folding in polypeptides of diversified molecular tacticity: Implications for protein folding and de novo design

Stereochemistry could be a powerful variable for conformational tune up of polypeptides for de novo design. It may be also useful probe of possible role of interamide energetics in selection and stabilization of conformation. The homopolypeptides Ac-Xxx(30)-NHMe, with Xxx = Ala, Val, and Leu, of diversified stereochemical structure are generated by simulated racemization with a modified GROMOS-96 force field The polypeptides, and other systematic stereochemical variants, are folded by simulated annealing with another modified GROMOS-96 force field under the dielectric constant values 1, 4, and 10. The resultant 15,000 molecular folds of isotactic (poly-L-chiral), syndiotactic (alternating L,D-chiral), and heterotactic (random-L,D-chiral) stereochemical structure, belonging to three polypeptide series, achieved under three different folding conditions, are assessed statistically for structure-to-energy-to-conformation relationship. The results suggest that interamide electrostatics could be a major factor in secondgry-structure selection in polypeptides while main-chain stereochemistry could dictate molecular packing and therefore the relative magnitude of hydrogen-bond and Lennard-Jones (LJ) contributions in conformational energy. A method for computational design of heterotactic molecular folds in polypeptide structure has been developed, and the first road map for a chiral tune up of polypeptide structure based on stereochemical engineering has been laid down. Broad implications for protein structure, folding, and de novo design are briefly discussed © 2005

Crystal structures of heterochiral peptides .2. tert-Boc-valyl-D-alanyl-leucyl-alanyl methoxide

Crystal structure of a heterochiral peptide, viz. Bac-Val(1)-D-Ala(2)-Leu(3)-Ala(4)-OMe with a D chiral residue in the second position of a sequence, has been determined [a = 40.44(1), b = 4.887(5), c = 15.381(5) Angstrom, beta = 109.6(1)degrees, space group C2, Z = 4, R = 0.11]. The peptide is in a parallel beta-sheet structure terminated by a distinct local bend. The structure is stabilised by N-H ... O as well as C-alpha-N ... O hydrogen bonds,The contiguous C-alpha-H ... O hydrogen bond observed in this structure is an unique observation. (C) Munksgaard 1997