Abstract: The present invention includes compositions and methods for the use of an encapsulation additive having between about 0.1 to about 30 percent isolated and purified vitelline protein B to provide for mixed and extended release formulations.

Abstract: The present invention includes compositions and methods for the use of an encapsulation additive having between about 0.1 to about 30 percent isolated and purified vitelline protein B to provide for mixed and extended release formulations.

Abstract: The present invention includes compositions and methods for the use of an encapsulation additive having between about 0.1 to about 30 percent isolated and purified vitelline protein B to provide for mixed and extended release formulations.

Abstract: Methods for making self-healing polymer and gel compositions with crosslinks comprising coordinate bonds between monomer subunits and metals are disclosed.

Abstract: The present invention includes compositions and methods for the use of an encapsulation additive having between about 0.1 to about 30 percent isolated and purified vitelline protein B to provide for mixed and extended release formulations.

Abstract: A system for integrating multiple software modules configured to produce output according to established business rules is provided. The system in one embodiment coordinates the printing of a variety of labels and reports according to a set of complex business rules. Complex output tasks may be distributed to remote computers in a network for optimum efficiency. The system may be configured to comply with one or more standard database connectivity standards in order to provide a generic interface with foreign systems. The method in one embodiment includes acquiring an input, sending a query to a database, retrieving business rules and associated tasks, and building scripts or commands for each task. This Abstract is provided to comply with the rules, which require an abstract to quickly inform a searcher or other reader about the subject matter of the application. This Abstract is submitted with the understanding that it will not be used to interpret or limit the scope or meaning of the claims.

Abstract: A water-resistant polyphenolic protein adhesive has been obtained from the Atlantic ribbed mussel, Geukensia (Modiolus) demissa. This protein provides a natural model for synthetic or bioengineered adhesives and is characterized by a Gly-Tyr-Lys or, more frequently, Gly-Dop-Lys "tail" fragment of a repeating octapeptide or nonapeptide unit. A complete octapeptide or nonapeptide unit (including both the 5- or 6-amino acid residue "head" as well as the 3-residue "tail") can be represented as follows:[Gln]Glu].sub.x -Thr/Ala-Gly-Dop/Tyr-Y.sup.1 -Y.sup.2 -Gly-Tyr/Dop-Lyswhere x is zero or one,Y.sup.1 is Val, Leu, Asp or Ser, andY.sup.2 is Ala, Pro, Hyp, or Leu.The tripeptide "tail" and/or the 5- or 6-residue "head" of the polypeptide is useful as a single unit (curable with difunctional crosslinkers or the like) or as a repeating unit.

Abstract: Methods are described for the preparation and isolation of novel decapeptides of the formula: ##STR1## wherein each X is independently selected from the group comprising hydroxyl and hydrogen, wherein each R is independently selected from the group comprising hydrogen and methyl, from bioadhesive polyphenolic proteins which comprise: ##STR2## wherein n is a whole number from about 60 to about 100, wherein each X is independently selected from the group comprising hydroxyl and hydrogen, and wherein each R is independently sselected from the group comprising hydrogen and methyl.Such decapeptides may be used to construct large polyphenolic molecules comprising from about 1 to about 1000 decapeptide repeating units and wherein the linking group is selected from the group comprising amino acid, oligopeptide and bifunctional spacer.

Abstract: Methods are described for the preparation and isolation of novel decapeptides of the formula: ##STR1## wherein each X is independently selected from the group comprising hydroxyl and hydrogen, wherein each R is independently selected from the group containing hydrogen and methyl, from bioadhesive polyphenolic proteins which comprise: ##STR2## wherein n is a whole number from about 60 to about 100, wherein each X is independently selected from the group comprising hydroxyl and hydrogen, and wherein each R is independently selected from the group comprising hydrogen and methyl.Such decapeptides may be used to construct large polyphenolic molecules comprising from about 1 to about 1000 decapeptide repeating units and wherein the linking group is selected from the group comprising amino acid, oligopeptide and bifunctional spacer.

Abstract: Methods are described for the preparation and isolation of novel decapeptides of the formula: ##STR1## wherein each X is independently selected from the group comprising hydroxyl and hydrogen, wherein each R is independently selected from the group comprising hydrogen and methyl, from bioadhesive polyphenolic proteins which comprise: ##STR2## wherein n is a whole number from about 60 to about 100, wherein each X is independently selected from the group comprising hydroxyl and hydrogen, and wherein each R is independently selected from the group comprising hydrogen and methyl.Such decapeptides may be used to construct large polyphenolic molecules comprising from about 1 to about 1000 decapeptide repeating units and wherein the linking group is selected from the group comprising amino acid, oligopeptide and bifunctional spacer.

Abstract: A process is provided for purifying and stabilizing marine mussel polyphenolic proteins rich in 3,4-dihydroxyphenylalanine (dopa) and hydroxyproline (hyp) while obtaining high yields thereof. The process includes the steps of providing an acid soluble extract of the dopa-containing proteins, removing the low molecular weight material from the extract and reacting the remaining proteinaceous material with a water soluble borate at a pH of 7.0-9.0 to provide a soluble borate complex of the dopa-containing protein while precipitating impurities. The complex is separated from the precipitate and may be concentrated for storage or treated with an acetic acid solution and either concentrated or lyophilized and stored under an inert atmosphere. The purified proteins exhibit a dopa:protein index of purity ratio of at least about 0.10.