A comparative study of two layer versus three-layer repair of mediolateral episiotomy

Background: Since majority of the women attending study hospital are belonging to lower socioeconomic strata and active involvement of paramedical staff in providing obstetric care, this study was undertaken to find the utility of a two-layer repair of mediolateral episiotomy and compare it with the standard method of closure in relation to its simplicity, cost-effectiveness and superiority if any, over the traditional three-layered repair of episiotomy.Methods: This was a prospective interventional study comparing 100 women who underwent two-layer closure with 100 women who underwent three-layer closure of episiotomy in a tertiary care hospital in Pune, India over a period of 2 years from October 2012 to October 2014. The parameters assessed were operative time, number of suture materials required, immediate post procedure pain and complications at follow-up. Qualitative and quantitative data was analysed using unpaired t-test, chi square test and Fisher exact test.Results: Both the groups were comparable in terms of hospital stay and wound complications such as oedema, dehiscence, hematoma, requirement of resuturing, cosmesis and long-term complications such as dyspareunia. However, two-layer repair required less operative time, lesser number of suture materials and decreased pain during hospital stay as there was statistically significant difference observed between the two groups.Conclusions: In this study experience, it can be concluded that two-layer repair of episiotomy is faster, with less post-operative pain and more cost effective. Hence it provides mother with better services

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

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

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

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

Conformational preferences of heterochiral peptides. Crystal structures of heterochiral peptides Boc-(D) Val-(D) Ala-Leu-Ala-OMe and Boc-Val-Ala-Leu-(D) Ala-OMe- enhanced stability of beta-sheet through C-H - O hydrogen bonds

The crystal structures of Boc-(D) Val-(D) Ala-Leu-Ala-OMe (vaLA) and Boc-Val-Ala-Leu-(D) Ala-OMe (VALa) have been derermined. vaLA crystallises in space group P2(1)2(1)2(1) with a = 9.401 (4), b = 17.253 (5). c = 36.276 (9)Angstrom, V = 5884 (3) Angstrom (3), Z = 8, R = 0.086. VALa crystallises in space group p2(1)2(1)2(1) with a = 9.683 (9), b = 17.355 (7), c = 18.187 (9) Angstrom, beta = 95.84 (8)degrees, V = 3040(4) Angstrom (3), Z = 4. R = 0.125. There are two molecules in the asymmetric unit in antiparallel P-sheet arrangement in both the structures. Several of the Ca hydrogens are in hydrogen bonding contact with the carbonyl oxygen in the adjacent strand. An analysis of the observed conformational feature of D-chiral amino acid residues in oligopeptides. using coordinates of 123 crystal structures selected from the 1998 release of CSD has been carried out. This shows that all the residues except D-isoleucine prefer both extended and a, conformation though the frequence of occurence may not be equal. In addition to this, D-leucine, valine, proline and phenylalanine have assumed cc, conformations in solid slate. D-leucine has a strong preference for helical conformation in linear peptides whereas they prefer an extended conformation in cyclic peptides

A SINGLE-POINT CHIRAL INVERSION THAT SELFORGANIZES A RANDOMCOIL PEPTIDE - APOLAR SOLVENT CONFORMATION OF BOC-(L-BACKSLASH-D)-GLU-ALA-LEU-LYSNHME

The tetrapeptide Boc-L-Glu-Ala-Leu-LysNHMe (1) reveals a random coil conformation, based on its Glu(gamma) and Lys(epsilon) methylene proton aniosotropic shift, GluNH chemical shift, NOEs in chloroform-DMSO (6:1), and its amide proton temperature coefficients in DMSO, while on similar considerations, the diastereomer Boc-D-Glu-Ala-Leu-LysNHMe (2) is characterized as a highly ordered 3/10 type distorted protohelix with a remarkably stable intramolecular salt bridge under these solvent conditions

Creating novel protein scripts beyond natural alphabets

Natural proteins are concatenated amino acids with definite handedness or chirality, with their spatial orientation being preferentially left handed or L-chiral. This paper discusses the biophysics of stereo-chemical perturbation to proteins using D-(α) amino acid and its utility as an additional design alphabet while scripting novel protein structures