Laparoscopic liver sectionectomy 2 and 3 (LLS 2 and 3): towards the "gold standard".

BACKGROUND: The purpose of this article is to define the state of the art in laparoscopic liver sectionectomy 2 and 3 (LLS 2 and 3) in order to advance the good option towards the "gold standard". METHODS: Based on a large review of the literature as well as on our personal experience the authors define clearly: the feasibility and the effectiveness of LLS 2 and 3. RESULTS: In this review the conversion rate was <4%, the histological positive margins was <0.8%, and the mortality was inferior to 0.8%. CONCLUSION: The LLS 2 and 3 seem equivalent or perhaps better option compared with the same intervention performed by laparotomy and can be proposed as primary with a grade C recommendation.

Synthesis of a new insoluble polymer-supported chiral alcohol auxiliary and its first application to nucleophilic addition to ketenes.

The preparation of a new optically active alcohol with a carboxylic function that allowed its attachment to an amine-functionalized insoluble polymer is described. Its first use as a polymer supported chiral auxiliary is demonstrated by asymmetric transformation of two racemic aryl propionic acids via ketene formation (95-96% ee).

[New derivatives of pantolactonyl N-phthalimido-2-arylpropanoate]. / Nouveau dérivés de N-phtalimido-2-arylepropanoate de pantolactonyle.

We present the crystal and molecular structures of two new N-phthalyl-3-amino-2-arylpropionic acid pantolactonyl ester derivatives with 4-fluorophenyl and 3,4-dimethoxyphenyl as the aryl group, 2,3,4,5-tetrahydro-4,4-dimethyl-2-oxofuran-3-yl 3-phthalimido-2-(4-fluorophenyl)propanoate, C23H20FNO6, and 2,3,4,5-tetrahydro-4,4-dimethyl-2-oxofuran-3-yl 3-phthalimido-2-(3,4-dimethoxyphenyl)propanoate ethyl acetate hemisolvate, C25H25NO8.0.5C4H8O2. This structural study confirms the S configuration of the C2 and validates the stereospecificity of our synthesis strategy.

Synthesis and characterization of bradykinin B(2) receptor agonists containing constrained dipeptide mimics.

We have previously shown that substitution of the D-Tic-Oic dipeptide by a (3S)-[amino]-5-(carbonylmethyl)-2,3-dihydro-1, 5-benzothiazepin-4(5H)-one (D-BT) moiety in the bradykinin B(2) receptor antagonist HOE 140 resulted in a full potent and selective bradykinin B(2) receptor agonist (H-DArg-Arg-Pro-Hyp-Gly-Thi-Ser-D-BT-Arg-OH, JMV1116) exhibiting a high affinity for the human receptor (K(i) 0.7 nM). In the present study, we have investigated the effects of replacement of the D-Tic-Oic moiety by various constrained dipeptide mimetics. The resulting compounds were tested for their binding affinity toward the cloned human B(2) receptor and for their functional interaction with the bradykinin-induced contraction of isolated human umbilical vein. Subsequently, we have designed novel bradykinin B(2) receptor agonists which are likely to be resistant to enzymatic cleavage by endopeptidases and which might represent interesting new pharmacological tools. In an attempt to increase the potency of compound JMV1116, both its N-terminal part and the D-BT moiety were modified. Substitution of the D-arginine residue by a L-lysine residue led to a 10-fold more potent bradykinin B(2) ligand [compound 22 (JMV1465) (K(i) 0.07 nM)], retaining full agonist activity on human umbilical vein. Substitution of the D-BT moiety by a (3S)-[amino]-5-(carbonylmethyl)-2,3-dihydro-8-methyl-1, 5-benzothiazepin-4(5H)-one [D-BT(Me)] moiety led to compound 23 (JMV1609) which exhibited a higher agonist activity (pD(2) = 7.4) than JMV1116 (pD(2) = 6.8).

How to build optically active alpha-amino acids.

Various methodologies published in the literature dealing with alpha-amino carboxylic acid asymmetric synthesis are presented in a digest form. In each case, only some recent or most typical works are mentioned.

Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins.

Some of the chemistry of amino acids going on in our laboratory (Laboratoire des Amino acides Peptides et Protéines) is described as well as some mass spectrometry methodology for their characterization particularly on solid supports. Several aspects are presented including: (i) the stereoselective synthesis of natural and unnatural amino acids using 2-hydroxypinan-3-one as chiral auxiliary; (ii) the stereoselective synthesis of natural and unnatural amino acids by deracemization of alpha-amino acids via their ketene derivatives; (iii) the synthesis of alpha-aryl-alpha-amino acids via reaction of organometallics with a glycine cation; (iv) the diastereoselective synthesis of glycosyl-alpha-amino acids; (v) the synthesis of beta-amino acids using alpha-aminopyrrolidinopiperazinediones as chiral templates; (vi) the reactivity of urethane-N-protected N-carboxyanhydrides. To characterize natural and non natural amino acids through their immonium ions by mass spectrometry, some methodology is also described.

Use of a new sonically cleavable and acido-labile handle for solid-phase peptide amide synthesis.

A new handle usable for solid-phase peptide amide synthesis was designed. New releasing conditions of the peptide using sonication allowed much shorter reaction times at lower TFA concentrations.

Synthesis and biological activity of a destruxin analogue: D-Lac-6 destruxin E.

A general strategy for the synthesis of destruxin analogues is described and applied to a particular example, D-Lac-6 destruxin E. The tetrapeptide Boc-Ile-N-MeVal-N-MeAla-beta-Ala-OMe (2) was chosen as the basic starting compound, and its preparation was optimized. This fragment was then coupled with the compound (D)Lac-Pro, and the resulting peptide was cyclized by the DEPC or DPPA/HOBt/DMAP methods at 21 and 30% yield, respectively. The biological activity of the analogue obtained was established by injection to an insect host.

SS-A (Ro) antibody in random mother-infant pairs.

In a study of the occurrence of detectable antibodies to SS-A and SS-B in 300 randomly selected mother-infant pairs, three (1%) mother-infant pairs were positive for precipitating antibodies to SS-A. No matched pairs were positive for SS-B. Review of the clinical history of the mother-infant pairs with SS-A antibodies failed to reveal evidence of connective tissue disease or the neonatal lupus syndrome. Follow up of two of the three SS-A positive mother-infant pairs two months after delivery also showed no evidence of disease. While the SS-A antibody may be closely associated with the development of the neonatal lupus syndrome, our study does not support the proposed aetiological nature of the antibody. Random maternal screening for possible SS-A antibody positivity and potential neonatal lupus syndrome does not appear to be warranted.