Human Islet Amyloid Polypeptide (hIAPP)-Binding D-Enantiomeric Peptides for the Treatment of Type 2 Diabetes Mellitus

Simple SummaryContent extracted from patent full text and abstract with AI.

This invention covers a set of D-enantiomeric peptides (composed of mirror-image amino acids) that are designed to bind to human islet amyloid polypeptide (hIAPP), a protein implicated in the destruction of insulin-producing beta cells in the pancreas. In Type 2 diabetes, hIAPP misfolds and aggregates into toxic amyloid fibrils, contributing to beta-cell loss and disease progression. The described peptides, defined by specific amino acid sequences (SEQ ID NO: 1–7) as well as their homologues and fragments, are intended to interfere with this aggregation process. Because they are built from D-amino acids, they are highly resistant to enzymatic degradation in the body, making them more stable than conventional peptide drugs.

Use CasesContent extracted from patent full text and abstract with AI.

• Treatment of Type 2 diabetes mellitus by inhibiting hIAPP amyloid fibril formation in the pancreatic islets of Langerhans.
• Development of therapeutic peptide drugs that protect insulin-producing beta cells from amyloid-induced toxicity in diabetic patients.
• Use as research tools to study hIAPP aggregation mechanisms and screen for further anti-amyloid compounds in diabetes drug discovery programs.
• Formulation into stable pharmaceutical preparations (e.g., injectable or oral) benefiting from the protease-resistance of D-amino acid peptides.
• Potential application in preventing or slowing beta-cell decline in pre-diabetic individuals at high risk of progressing to Type 2 diabetes.

BenefitsContent extracted from patent full text and abstract with AI.

• D-enantiomeric composition confers high resistance to proteolytic degradation, resulting in significantly longer in vivo half-life compared to conventional L-amino acid peptides.
• Targeted binding to hIAPP inhibits toxic amyloid aggregation, directly addressing a key pathological mechanism of Type 2 diabetes rather than merely managing symptoms.
• Mirror-image peptides are less likely to trigger immune responses, improving the safety profile relative to standard peptide therapeutics.
• Defined sequence variants (SEQ ID NO: 1–7) plus homologues and fragments provide a broad structural basis for optimizing binding affinity and selectivity.
• Peptide-based modality allows precise molecular targeting of hIAPP aggregation intermediates that are difficult to address with small-molecule drugs.

Technical Classifications (CPCs)

Inventors & Applicants

Patent Abstract

Described is a peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6 and SEQ ID NO: 7 as well as homologues, fragments and parts thereof.