Abstract
Human insulin (HI) is a well-characterized natural hormone which regulates glycose levels into the blood-stream and is widely used for diabetes treatment. Numerous studies have manifested that despite significant efforts devoted to structural characterization of this molecule and its complexes with organic compounds (ligands), there is still a rich diagram of phase transitions and novel crystalline forms to be discovered. Towards the improvement of drug delivery, identification of new insulin polymorphs from polycrystalline samples, simulating the commercially available drugs, is feasible today via macromolecular X-ray powder diffraction (XRPD). This approach has been developed, and is considered as a respectable method, which can be employed in biosciences for various purposes, such as observing phase transitions and characterizing bulk pharmaceuticals. An overview of the structural studies on human insulin complexes performed over the past decade employing both synchrotron and laboratory sources for XRPD measurements, is reported herein. This review aims to assemble all of the recent advances in the diabetes treatment field in terms of drug formulation, verifying in parallel the efficiency and applicability of protein XRPD for quick and accurate preliminary structural characterization in the large scale.
Highlights
Diabetes mellitus (DM), was one of the first diseases ever described [1], whereas its name, was originated from the Greek word “diabaino” (=passing through referring to the great emptying of the urine) and “meli” (=honey referring to the sweet taste of the patientsurine due to high glucose concentration)
The present review reports recent research advances of insulin-based polycrystalline compounds compounds as potential therapeutics against diabetes
The majority of structural studies reported as potential therapeutics against diabetes
Summary
Diabetes mellitus (DM), was one of the first diseases ever described [1], whereas its name, was originated from the Greek word “diabaino” (=passing through referring to the great emptying of the urine) and “meli” (=honey referring to the sweet taste of the patientsurine due to high glucose concentration). Results include the structural characterization of HI in the presence or absence of small organic molecules (ligands) in a wide pH range (~4.5–8.5) obtained via XRPD, including the identification of four previously unknown insulin polymorphs: C2221 , C2, P21(α) and P21(γ) [29,53,54,55,56]. These studies indicate that there is still a rich diagram of human insulin phase transitions, as well as novel crystalline phases to be discovered
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