Qbd analytical development of calcitonin bioadhesive formulation

Calcitonin is a 32-amino acid polypeptide hormone ubiquitous in humans and animals. It acts i.a. to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH). Both human (hu) and salmon (sa) calcitonins are clinically effective and currently approved as active pharmaceutical ingredients (APIs). A new bioadhesive nasal formulation is currently under development, which contains low dose calcitonin in polymeric excipients (carbomer and starch). The analytical development is confronted with several challenges: the low dose of the peptide in the formulation, its inherent instability, the polymeric matrix interacting with the peptide influencing sample preparation and its undefined degradation impurity profile in this formulation. The aim of this investigation was to develop a suitable method to determine the concentration of sa-calcitonin in this formulation and to establish its degradation profile, using experimental designs which will also give us mechanistic information. Degradation profiling was developed towards the sensitive detection of all possible already-identified related compounds [1], using a selective gradient FA-based RP-HPLC with ESI/iontrap MS detection in the SIM mode The assay was developed using Onion and Plackett-Burman designs, evaluating and optimizing the sample treatment procedure. The chromatography method is based on a TFA-based gradient RP-HPLC with UV detection for quantification. Both methods are applied in short-term stability studies for the release of clinical trial material

Isolation and Immunocytochemical Characterization of Three Tachykinin-Related Peptides from the Mosquito, Culex salinarius

Three myotropic peptides belonging to the Arg-amide insect tachykinin family were isolated from whole-body extracts of the mosquito, Culex salinarius . The peptides, APSGFMGMR-NH 2 , APYGFTGMR-NH 2 and APSGFFGMR-NH 2 (designated culetachykinin I, II, and III) were isolated and purified on the basis of their ability to stimulate muscle contractions of isolated Leucophaea maderae hindgut. Biologically inactive methionine sulfoxides of two of the three peptides were isolated using an ELISA system based upon antiserum raised against APYGFTGMR-NH 2 and identified with mass spectrometry. Immunocytochemistry localized these peptides in cells in the brain, antennae, subesophageal, thoracic and abdominal ganglion, proventriculus and midgut. Nerve tracts containing these peptides were found in the median nerve of the brain, central body, nervi corpus cardiaci, cervical nerve, antennal lobe and on the surface of the midgut.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45417/1/11064_2004_Article_419298.pd

The evolution and nomenclature of GnRH-type and corazonin-type neuropeptide signaling systems

The work of the authors reported in this review was supported by grants from the BBSRC (BB/M001644/1; BB/M001032/1), the Leverhulme Trust (RGP-2013-351) and the China Scholarship Council

Proportionaliteit van stemrecht en risico in kapitaalvennootschappen.

status: publishe

Proportionaliteit van stemrecht en risico in kapitaalvennootschappen.

De materie werd bijgehouden tot 1 februari 201