Compositions comprising tri- and penta-block synthetic copolypeptide hydrogels
AssigneeThe Regents of the University of California
InventorsTimothy J. Deming, Yintao Sun
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Abstract
Disclosed herein are mixtures of triblock or pentablock copolypeptide hydrogels (DCH). These hydrogels possess improved mechanical properties, such as elasticity, that are synergistically increased over the individual component DCHs, to greater than would be expected for a linear combination of the components. Also disclosed herein are methods of making and using the triblock and pentablock copolypeptide hydrogels.
Claims43
A composition comprising:
- i) a first copolypeptide comprising Substructure I, and a second copolypeptide comprising Substructure II, and water, wherein
- Substructure I is depicted as follows:
- -A1n1-B1m1-A1n1- Substructure I;
- Substructure II is depicted as follows:
- —X1n2—Y1m2—X1n2— Substructure II;
- each instance of A1 is an amino acid residue independently selected from a non-ionic hydrophilic amino acid, sarcosine, glycine, and alanine;
- in at least 20% of the instances of B1, B1 is an amino acid residue independently selected from an anionic hydrophilic amino acid or a salt thereof;
- each instance of X1 is an amino acid residue independently selected from a non-ionic hydrophilic amino acid, sarcosine, glycine, and alanine;
- in at least 20% of the instances of Y1, Y1 is an amino acid residue independently selected from a cationic hydrophilic amino acid or a salt thereof;
- each n1 and n2 is independently about 25 to about 600;
- m1 and m2 are independently about 15 to about 600;
- at least 75 mol % of the B1 amino acid residues are (D)-amino acid residues or at least 75 mol % of the B1 amino acid residues are (L)-amino acid residues;
- at least 75 mol % of the Y1 amino acid residues are (D)-amino acid residues or at least 75 mol % of the Y1 amino acid residues are (L)-amino acid residues;
- and
- the first copolypeptide and the second copolypeptide are not covalently linked;
- or
- ii) Substructure III, and a second copolypeptide comprising Substructure IV, and water, wherein Substructure III is depicted as follows:
- -A1n1-B1m1-A1n3-B1m1-A1n1- Substructure III:
- Substructure IV is depicted as follows:
- —X1n2—Y1m2—X1n4—Y1m2—X1n2— Substructure IV;
- each instance of A1 is an amino acid residue independently selected from a non-ionic, hydrophilic amino acid, sarcosine, glycine, and alanine;
- in at least 20% of the instances of B1, B1 is an amino acid residue independently selected from an anionic hydrophilic amino acid or a salt thereof;
- each instance of X1 is an amino acid residue independently selected from a non-ionic hydrophilic amino acid, sarcosine, glycine, and alanine;
- in at least 20% of the instances of Y1, Y1 is an amino acid residue independently selected from a cationic hydrophilic amino acid or a salt thereof;
- each n1, n2, n3, and n4 is independently about 25 to about 600;
- each m1 and m2 is independently about 15 to about 600;
- at least 75 mol % of the B1 amino acid residues are (D)-amino acid residues or at least 75 mol % of the B1 amino acid residues are (L)-amino acid residues;
- at least 75 mol % of the Y1 amino acid residues are (D)-amino acid residues or at least 75 mol % of the Y1 amino acid residues are (L)-amino acid residues;
- and
- the first copolypeptide and the second copolypeptide are not covalently linked.
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Dependencies are inferred from the claim text.