The invention relates to a microparticulate system for the delayed and controlled release of active principles (AP) whose absorption window in vivo is essentially limited to the upper parts of the gastrointestinal tract, this system being intended for oral administration The object of the invention is to provide a system ensuring that the AP is released with certainty by means of a dual mechanism of “time-dependent” and “pH-dependent” release To achieve this object, the invention proposes a multimicrocapsular oral galenical form which is designed so as to guarantee therapeutic efficacy, and in which the release of the AP is governed by a dual release triggering mechanism that is “time-triggering” and “pH-triggering” This system comprises of microcapsules (200 to 600 μm) comprising a core of AP coated with a film (maximum 40% by weight) comprising a hydrophilic polymer A (Eudragit® L) and a hydrophobic compound B (vegetable wax, melting point=40-90° C), B/A being between 02 and 15 These microcapsules have a dissolution behavior in vitro such that, at a constant pH of 14, a latency phase of between 1 and 5 hours is observed, followed by a release of the AP, and such that the change from pH 14 to pH 68 results in a release of the AP without a latency period in vitro

Microparticulate oral galenical form for the delayed and controlled release of pharmaceutical active principles

From t/c values measured at 25 °C for the series Ac-Hel1-An-OH, n = 1−6 in D2O the helical propagation constant (s value) for alanine in this templated peptide series is 1.03; the corresponding value in 10 mol % trifluoroethanol−D2O is 1.47. An iterative least squares analysis for calculating s values from t/c ratios is developed, errors implicit in its application are discussed, and the s value is related to the degree of helical fraying.

The structure and energetics of helix formation by short templated peptides in aqueous solution. 3. calculation of the helical propagation constant s from the template stability constants t/c for ac-hel1-alan-oh, n = 1-6

In this paper, we describe the design and implementation of a message-passing algorithm which enables the Empirical Conformational Energy Program for Peptides (ECEPP/3) and related programs to run efficiently on the IBM RISC System/6000 POWERparallel System (SP2). Either the Message Passing Library (MPL) or the Message Passing Interface (MPI) can be used on the SP2; the MPI version also runs on the SGI Power Challenge computer. Some performance data are presented.

Implementation of ECEPP-Based Programs on the IBM SP2 and the SGI Power Challenge Computers

Preparation, caracterisation et etude par spectrometrie de dichroisme circulaire de la transition helice-pelote des copolymeres Leurs courbes de fusion calculees a partir d'une theorie de transition helice-pelote ne correspondant pas aux courbes experimentales, cette theorie est etendue en considerant l'effet des interactions dues au motif voisin La theorie ainsi modifiee rend compte les resultats experimentaux

Helix-coil transition in multicomponent random copolypeptides in water. 3. Inclusion of nearest-neighbor interactions and application to random copolymers of (hydroxybutyl)-L-glutamine, L-alanine, L-phenylalanine, L-lysine, and glycine

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Helix-coil transition in multicomponent random copolypeptides in water. 3. Inclusion of nearest-neighbor interactions and application to random copolymers of (hydroxybutyl)-L-glutamine, L-alanine, L-phenylalanine, L-lysine, and glycine