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

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.