Team:Sydney Australia/Patent Law

GENERAL HEADER ON OUR PATENTS

Although our team attempted to be thorough, 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 claims from patents are not illegal so long as we do not directly market this product which our team is not pursuing at this stage.

DIMARCHI ET AL.

Single Chain Insulin with high bioactivity

Patent No: US 9458,220 B2

October 4th 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 7th 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 30th 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 – UI – Zn – Y – ZI – Un – 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
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