Acta Diabetologica

, Volume 55, Issue 5, pp 405–418 | Cite as

Advances in micro- and nanotechnologies for the GLP-1-based therapy and imaging of pancreatic beta-cells

  • Faruk H. Moonschi
  • Corey B. Hughes
  • George M. Mussman
  • John L. Fowlkes
  • Chris I. Richards
  • Iuliana Popescu
Review Article


Therapies to prevent diabetes in particular the progressive loss of β-cell mass and function and/or to improve the dysregulated metabolism associated with diabetes are highly sought. The incretin-based therapy comprising GLP-1R agonists and DPP-4 inhibitors have represented a major focus of pharmaceutical R&D over the last decade. The incretin hormone GLP-1 has powerful antihyperglycemic effect through direct stimulation of insulin biosynthesis and secretion within the β-cells; it normalizes β-cell sensitivity to glucose, has an antiapoptotic role, stimulates β-cell proliferation and differentiation, and inhibits glucagon secretion. However, native GLP-1 therapy is inappropriate due to the rapid post-secretory inactivation by DPP-4. Therefore, incretin mimetics developed on the backbone of the GLP-1 or exendin-4 molecule have been developed to behave as GLP-1R agonists but to display improved stability and clinical efficacy. New formulations of incretins and their analogs based on micro- and nanomaterials (i.e., PEG, PLGA, chitosan, liposomes and silica) and innovative encapsulation strategies have emerged to achieve a better stability of the incretin, to improve its pharmacokinetic profile, to lower the administration frequency or to allow another administration route and to display fewer adverse effects. An important advantage of these formulations is that they can also be used at the targeted non-invasive imaging of the beta-cell mass. This review therefore focuses on the current state of these efforts as the next step in the therapeutic evolution of this class of antidiabetic drugs.


Microparticles Nanoparticles Incretins GLP-1 Beta-cell Diabetes 


Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Informed consent

For this type of study, formal consent is not required.

Supplementary material

592_2017_1086_MOESM1_ESM.pdf (127 kb)
Supplementary material 1 Molecular structures of the human GLP-1(7-37) (a) and GLP-1 analogs (b–g) approved on the market, modified after Manandhar B [61] Nauck M [64] and Glaesner W [65]. (b) Exenatide; (c) lixisenatide; (d) liraglutide; e) semaglutide; (f) albiglutide; (g) dulaglutide. The colors identify differences between the amino acid sequence or/and other moieties within the peptide structure (PDF 128 kb)


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Copyright information

© Springer-Verlag Italia S.r.l., part of Springer Nature 2017

Authors and Affiliations

  • Faruk H. Moonschi
    • 1
  • Corey B. Hughes
    • 2
  • George M. Mussman
    • 2
  • John L. Fowlkes
    • 2
  • Chris I. Richards
    • 1
  • Iuliana Popescu
    • 2
  1. 1.Department of ChemistryUniversity of KentuckyLexingtonUSA
  2. 2.Barnstable Brown Kentucky Diabetes CenterUniversity of KentuckyLexingtonUSA

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