Methods for aggregation of proteins

A method for down-regulating the biological function of a protein, comprising

• (a) contacting the protein with a molecule of structure (B), (C), (D), or (E):
• (B) Z0—X1—Y1—X2—Z1—X3—Y2—X4—Z2, wherein Z1 is a linker and Z2 is selected from a linker or nothing,
• (C) Z0—X1—Y1—X2—Z1—X3—Y2—X4—Z2—X5—Y3—X6—Z3, wherein Z1 and Z2 are each independently a linker and Z3 is selected from a linker or nothing,
• (D) Z0—X1—Y1—X2—Z1—X3—Y2—X4—Z2—X5—Y3—X6—Z3—X7—Y4—X8—Z4, wherein Z1, Z2, and Z3 are each independently a linker and Z4 is selected from a linker or nothing,
• (E) Z0—X1—Y1—X2—Z1—X3—Y2—X4—Z2—X5—Y3—X6—Z0—Y4-X8—Z4—X0—Y5—X10—Z5, wherein Z1, Z2, Z3, and Z4 are each independently a linker and Z5 is selected from a linker or nothing
• wherein:
• Z0 is a linker or nothing,
• at least one of Y1, Y2, Y3, Y4, and Y5 is identical to, or differs by 1 or 2 amino acid substitutions from, a stretch of contiguous amino acids naturally occurring in the protein,
• X1, X2, X3, X4, X5, X6, X7, X8, X9, and X10 are independently selected from 1 to 4 contiguous amino acids selected from arginine (R), lysine (K), glutamatic acid (E), aspartic acid (D), or proline (P),
• Y1, Y2, Y3, Y4, and Y5, are independently selected from a stretch of 6 to 16 contiguous amino acids, wherein:
• at least 50% of the contiguous amino acids are hydrophobic amino acids,
• at least one aliphatic residue or phenylalanine (F) is present, and
• if only one aliphatic residue or F is present, then at least one other residue is selected from tyrosine (Y), tryptophan (W), alanine (A), methionine (M) and threonine (T), and each of Y1, Y2, Y3, Y4, and Y5 contains no more than 1 each of a P, R, K, D or E residue, and
• the molecule is devoid of a carrier or solubilizing moiety and
• (b) inducing co-aggregation with the protein, thereby down-regulating the biological function of the protein.