Technology Platform Description
Dr. Chen and colleagues have identified a 3 amino acid (AA) peptide (DT-109) that, when administered in combination with a glucose challenge, results in increased plasma insulin and glucagon-like 1 (GLP-1) levels and decreased blood glucose levels in both control and diabetic mouse models. This peptide is the most promising of 4 potential peptides that have similar activities. DT-109 is active in a dose-dependent manner in oral glucose tolerance tests.
The peptides synthesized and tested by Dr. Chen’s laboratory were glycine-glycine-leucine (GGL, DT-109), leucine-glycine-glycine (LGG), leucine-glycine-leucine (LGL), leucine-leucine-glycine (LLG), glycine-leucine-glycine (GLG), leucine-glycine-glycine (LGG), glycine-leucine-leucine (GLL), and glycine-glycine-histine (GGH).
The technology is unique in its application to the field of diabetes therapeutics; no other 3 amino acid peptides have been used as a treatment. In fact, the descriptions of 3 amino acid peptides in the scientific and patent literature are not related to any pharmaceutical usage. As such, the approach taken by Diapin Therapeutics is novel. The idea that amino acids and proteins can act to stimulate insulin secretion is not new. However, the use of a combination of amino acids in the form of short peptides for glycemic control is an inventive step in that it is not obvious that these peptides should have better activity than the amino acids from which they are derived. As with any invention, the composition and size of the peptides that will produce maximum activity remains to be established. However as the length of the peptide is increased beyond a certain limit, it is likely that its activity will diminish. Certain modifications to the N and C termini of the peptide, have not yielded increased activity to date. Diapin Therapeutics will continue to make modifications to DT-109 in hopes of identifying peptides with maximal insulin and incretin secretagogue activity.
The peptides synthesized and tested by Dr. Chen’s laboratory were glycine-glycine-leucine (GGL, DT-109), leucine-glycine-glycine (LGG), leucine-glycine-leucine (LGL), leucine-leucine-glycine (LLG), glycine-leucine-glycine (GLG), leucine-glycine-glycine (LGG), glycine-leucine-leucine (GLL), and glycine-glycine-histine (GGH).
The technology is unique in its application to the field of diabetes therapeutics; no other 3 amino acid peptides have been used as a treatment. In fact, the descriptions of 3 amino acid peptides in the scientific and patent literature are not related to any pharmaceutical usage. As such, the approach taken by Diapin Therapeutics is novel. The idea that amino acids and proteins can act to stimulate insulin secretion is not new. However, the use of a combination of amino acids in the form of short peptides for glycemic control is an inventive step in that it is not obvious that these peptides should have better activity than the amino acids from which they are derived. As with any invention, the composition and size of the peptides that will produce maximum activity remains to be established. However as the length of the peptide is increased beyond a certain limit, it is likely that its activity will diminish. Certain modifications to the N and C termini of the peptide, have not yielded increased activity to date. Diapin Therapeutics will continue to make modifications to DT-109 in hopes of identifying peptides with maximal insulin and incretin secretagogue activity.