Process Modelling for Control of Product Wall Thickness in Thermoforming

The present paper describes the results of an investigation into the modelling of plug assisted thermoforming. The objective of this work was to improve the finite element modelling of thermoforming through an enhanced understanding of the physical elements underlying the process. Experiments were carried out to measure the effects on output of changes in major parameters and simultaneously simple finite element models were constructed. The experimental results show that the process creates conflicting and interrelated contact friction and heat transfer effects that largely dictate the final wall thickness distribution. From the simulation work it was demonstrated that a high coefficient of friction and no heat transfer can give a good approximation of the actual wall thickness distribution. However, when conduction was added to the model the results for lower friction values were greatly improved. It was concluded that further work is necessary to provide realistic measurements and models for contact effects in thermoforming.

The complex array of bradykinin-related peptides (BRPs) in the peptidome of pickerel frog (Rana palustris) skin secretion is the product of transcriptional economy.

Previous peptidomic analyses of the defensive skin secretion from the North American pickerel frog, Rana palustris, have established the presence of canonical bradykinin and multiple bradykinin-related peptides (BRPs). As a consequence of the multiplicity of peptides identified and their diverse primary structures, it was speculated that they must represent the products of expression of multiple genes. Here, we present unequivocal evidence that the majority of BRPs (11/13) identified in skin secretion by the peptidomic approach can be generated by differential site-specific protease cleavage from a single common precursor of 321 amino acid residues, named skin kininogen 1, whose primary structure was deduced from cloned skin secretion-derived cDNA. The organization of skin kininogen 1 consists of a hydrophobic signal peptide followed by eight non-identical domains each encoding a single copy of either canonical bradykinin or a BRP. Two additional splice variants, encoding precursors of 233 (skin kininogen 2) or 189 amino acid residues (skin kininogen 3), were also cloned and were found to lack BRP-encoding domains 5 and 6 or 4, 5 and 6, respectively. Thus, generation of peptidome diversity in amphibian defensive skin secretions can be achieved in part by differential protease cleavage of relatively large and multiple-encoding domain precursors reflecting a high degree of transcriptional economy.