Difference between revisions of "Team:Sydney Australia/Patent Law"

Revision as of 12:16, 25 October 2017

GENERAL HEADER ON OUR PATENTS

Although our team attempted to be thorough with all the single chain patents, we recognise that not all patents can be checked. However, we targeted patents with the greatest relevance to avoid legal suits that may arise. Regardless, our work is for ‘research purposes’ in which an exception exists for patents under WHAT?? Testing of s from patents do not infringe an owner's property rights. So long as you do not attempt to market the product as your own or submit to an open registry; it is free to be used for characterisation etc.

DIMARCHI ET AL.

Single Chain Insulin with high bioactivity

Patent No: US 9458,220 B2

October 4^th 2016

CLAIM

COMPARISON WITH OUR SEQUENCE

Y/N

A single chain insulin agonist analogue with stricture of B-LM-A wherein B represents an insulin B chain comprising the sequence R₂₂X₂₅LCGX₂₉_… and A represents an insulin A chain comprising the sequence

GIVX₄X₅CCX₈_…-R₁₃

Both insulin A and B chains involve R groups which stand for modifications eg. carboxylation. As our insulin B chain does not contain any modifications (except an additional glycine at the A chain), our construct is outside the patent

N

Furthermore the linking moiety linking the carboxy terminus of the B chain to the amino terminus of the A chain; further wherein the linking moiety is an 8 amino acid sequence comprising of the sequence X₅₁X₅₂GSSSX₅₇X₅₈ wherein

X₅₁ = group consisting of glycine, alanine, valine, leucine, isoleucine, isoleucine and ornithine

X₅₂ = any amino acid other than tyrosine

X₅₇ and X₅₈ are independently selected form the ground consisting of arginine, lysine and ornithine

Our amino acid sequence is squarely outside the scope of 8 amino acids.

Even if we did fall within the claim; we do not contain the 8 amino acid sequence using both potential orientations

X₅₁ is glutamine or arginine in our sequence

B-chain – QR . . . RR – A-chain

N

The LM also requires the sequence of GAGSSSRR or a sequence that differs from GAGSSRR by 1 or 2 amino acids

Our sequence is 12 amino acids long and differs by more than 4 amino acids.

N

LM represents linking moiety linking the carboxyl terminus of the B chain to the amino terminus of the a chain, wherein said linking moiety is an 8 amino acid sequence consisting of X₅₁X₅₂X₅₃X₅₄... wherein X₅₁ is selected from the group consisting of glycine, alanine, valine, leucine, isoleucine and proline…

Similarly, the patent claim is over an 8 amino acid sequence. Applying the same principle our;

X₅₁ is glutamine or arginine (depending on orientation) and outside the scope

N

LEE ET AL.

Single Chain Insulin Analog and a polynucleotide sequence encoding the analog

Patent No: US 6,630,348 B1

October 7^th 2003

CLAIM	COMPARISON WITH OUR SEQUENCE	Y/N
A single chain insulin analogue compound of formula (I) having the properties of greater insulin receptor binding activity than proinsulin and less insulin receptor binding activity than insulin: B chain - X – A chain wherein:	General B – X – A chain single chain formula	Y
B and A chain are human insulin chains, respectively and,	Our B and A chain are human insulin chains although our A chain includes a modification (additional glycine)	N
X is a joining peptide of about 5 to 18 amino acids comprising the following sequence: Gly-Gly-Gly-Pro-Gly- Lys-Arg	Where the term ‘comprising’ is included, the patent requires that the specific sequence named MUST be part of the linker region. Although our sequence is 12 amino acids long, it does not contain the ‘GGGPGLR’ identified in the patent	N

LEE ET AL.

Single Chain Insulin Analogs

Patent No: EP 1 193 272 B1

October 30^th 2004

CLAIM

COMPARISON WITH OUR SEQUENCE

Y/N

A single chain insulin analogue compound of formula (I) having the properties of greater insulin receptor binding activity than prosinsulin and less insulin receptor binding activity than insulin:

B Chain – U_I – Z_n – Y – Z_I – U_n– A chain

B and A chain are human insulin chains respectively and

We have a modified A chain

N

U is an arginine or lysine residue

Our ‘U’ is glutamine

N

Z is a glycine

Z Is Glycine

Y

I is an integer of 2 – n

N is an integer of 0 or 2 and

The maximum size of the linker sequence when considering this is 9 amino acids. Since our sequence is 12 amino acids they are outside the scope

N

Y is glycine-proline-glycine, or alanine-proline-glycine-aspartic acid–valine, or tyrosine-proline-glycine-aspartic acid-valine, or histidine-proline-glycine-aspartic acid-valine.

Our sequence has no proline

N

KJELDSEN ET AL.

Single Chain insulin

Patent No: EP 1692168 B1

December 3^rd, 2004

CLAIM	COMPARISON WITH OUR SEQUENCE	Y/N
Single-chain insulin for treatment of type 1 diabetes and type 2 diabetes having the formula B(1-26)- X₁ - X₂ - X₃- X₄- A (1-21),	B - linker - A formula	Y
B(1-26) is a peptide chain consisting of the first 26 amino acid residues of the B chain of human insulin counted from the N-terminal end of the B chain or an analogue of the B-chain with one addition or one deletion of one of the amino acid residues in the B-chain or derivative of the B-chain being chemically modified by introducing a group in the side chain in one or more positions of the B-chain or by oxidation or reduction of the side chains of the amino acids residues in the B-chain,	Our B chain consists of 28 AA. Although the patents contain different versions eg ‘an analogue of the B-chain with one addition or deletion’ – the total length of the B-chain must STILL be 26AA.	N
and A(1-21) is the natural insulin A chain or an analogue thereof with one addition or one deletion of one of the amino acid residues in the A-chain or derivative of the A-chain being chemically modified by introducing a group in the side chain in one or more positions of the A-chain or by oxidation or reduction of the side chains of the amino acids residues in the A-chain, wherein	In our sequence construct – the A chain is 22 amino acids long. Just like in the B-chain (it only covers a TOTAL of 21 AA). Even though our A chain contains the addition of an amino acid (glycine), the length is too long for the patent to operate over.	N
X₄does not contain two adjacent basic amino acid residues and wherein the single-chain insulin has an affinity to the human insulin receptor of at least about 20% of that of human insulin if the single-chain insulin molecule is not chemically modified by acylation.	We have 2 adjacent basic amino acid residues and the affinity cannot be tested	N
wherein X₁ is Thr, Lys or Arg	X₁ is glutamine	N
X₂ is Pro, Lys or Asp,	X₂is arginine	N
X₃ is Lys, Pro or Glu,	X₃ is glycine	N
X₄ is a peptide sequence with the following formula X_a-X_b-X_c-X_d-X_e-X_fX_g (SEQ ID NO:129) wherein X_a is selected from the group consisting of L, R, T, A, H, Q, G, S and V; X_b is selected from the group consisting of W, G, S, A, H, R, and T; X_c is selected from the group consisting of L, Y, M, H, R, T, Q, K, V, S, A, G and P; X_d is selected from the group consisting of R, A, Y, M, S, N, H, and G; X_e is selected from the group consisting of S, R, A, T, K, P, N, M, H, Q, V, and G; X_f is selected from the group consisting of G and A; and X_g is selected from the group consisting of K, R, P, H, F, T, I, Q, W, and A,	The total linker length that can be formulated from X_a– X_g is 7 amino acids with the three other residues for X₁ – X₃. This totals to a maximum linker length of 10 amino acids. Our linker is 12 amino acids long.	N

WEISS ET AL.

Fibrillation-resistant insulin and insulin analogues
Patent No: EP 2074140 B1

April 6th, 2009

CLAIM	COMPARISON WITH OUR SEQUENCE	Y/N
An insulin analogue comprising a single chain polypeptide containing an insulin A-chain polypeptide and an insulin B-chain polypeptide connected by a truncated linker,	Our linker is truncated from the entire C-peptide to 12 amino acids and has the general formula of B-X-A where our linker is QRGGGSGGGQRR	Y
wherein the truncated linker is a polypeptide selected from the group consisting of:		Y
a polypeptide having the sequence GGGPRR	No proline	N
a polypeptide having the sequence GGPRR	No proline	N
a polypeptide having the sequence GSEQRR	No glutamate	N
a polypeptide having the sequence RREQR	No glutamate	N
a polypeptide having the sequence RREALQKR	No glutamate	N
a polypeptide having the sequence GAGPRR	No proline	N
a polypeptide having the sequence GPRR	No proline	N
wherein the insulin B-chain polypeptide optionally contains one or more of: an aspartate substitution at the position corresponding to position B10 of insulin, a lysine or an aspartate substitution at the position corresponding to position B28 of insulin, and a proline substitution at the position corresponding to position B29 of insulin	Our B-chain is native human insulin	N
and wherein the insulin A-chain polypeptide contains a histidine substitution at the position corresponding to position A8 of insulin.	Our A-chain does not contain the relevant substitution and only an additional glycine	N

STOWELL ET AL.

Chemically and thermodynamically stable insulin analogues and improved

methods for their production

Patent No: US 9006176 B2

October 16^th 2012

CLAIM	COMPARISON WITH OUR SEQUENCE	Y/N
A single chain insulin (SCI) compound of formula a(I): B chain - C’ – A Chain (Formula (I)) having the properties of higher affinity for the insulin receptor and lower affinity for the IGF-1 receptor as compared to those of native proinsulin with chemical and thermodynamic degradation profiles such that the SCI can be formulated and stored for extended periods of time without refrigeration;	Correct linker formulation of B-linker-A	Y
W herein B chain and A chain are modified human insulin chains; and		Y
Wherein C’ covalently links the C-terminus of the B chain to the N-terminus of the A chain, and is a peptide of 5 amino acids comprising the following sequence: Y-P-G-D-X (SEQ ID NO: 1); wherein X is any amino acid;	No proline (P) and no aspartic acid (D)	N
wherein the B chain is modified from a native human insulin B chain (SEQ ID NO:11), and A chain is modified from a native human insulin A chain (SEQ ID NO:10), wherein the modifications comprise one or more mutations at (1) Gln5, Gln15, Asn18, or Asn21 of SEQ ID NO:10, or (2) Asn3 or Gln5 of SEQ ID NO:11; resulting in enhanced resistance to deamidation.	B is not modified and A chain does not have similar modifications, rather an addition at residue 1 without the purpose of resisting deamination.	N

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