A comprehensive review on the research progress of PTP1B inhibitors as antidiabetics

Abstract

Diabetes mellitus (DM) is a serious global health concern affecting over 500 million people. To put it simply, it is one of the most dangerous metabolic illnesses. Insulin resistance is the root cause of 90% of all instances of diabetes, all of which are classified as Type 2 DM. Untreated, it poses a hazard to civilization since it can lead to terrifying consequences and even death. Oral hypoglycemic medicines presently available act in a variety of ways, targeting various organs and pathways. The use of protein tyrosine phosphatase 1B (PTP1B) inhibitors, on the contrary, is a novel and effective method of controlling type 2 diabetes. PTP1B is a negative insulin signaling pathway regulator; hence, inhibiting PTP1B increases insulin sensitivity, glucose absorption, and energy expenditure. PTP1B inhibitors also restore leptin signaling and are considered a potential obesity target. In this review, we have compiled a summary of the most recent advances in synthetic PTP1B inhibitors from 2015 to 2022 which have scope to be developed as clinical antidiabetic drugs.

Marine Compounds and Age-Related Diseases: The Path from Pre-Clinical Research to Approved Drugs for the Treatment of Cardiovascular Diseases and Diabetes

“…Sodium-Glucose Transport Protein 2 (SGLT2) inhibitors promote glucose urinary excretion. Inhibitors of the protein tyrosine phosphatase 1B (PTP1B), a negative regulator of the insulin signalling pathway, have emerged as a promising target for diabetes, but none have yet reached the market [102].…”

Identification of 1,3,4-Thiadiazolyl-Containing Thiazolidine-2,4-dione Derivatives as Novel PTP1B Inhibitors with Antidiabetic Activity

“…Therefore, PTP1B is a potential target for the T2DM treatment. Several naturally occurring and synthesized PTP1B inhibitors have been identified, − but none have been developed into clinical drugs. In the development process of PTP1B inhibitors, researchers have designed a lot of phosphorylated tyrosine (pTyr) mimetic as PTP1B inhibitors based on the catalytic domain structure of PTP1B, including derivatives of phosphoric acid, difluoromethyl phosphate, and carboxylic acid skeleton.…”