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New Perspectives on Drugs Targeting Lipid-Transfer Proteins
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New Perspectives on Drugs Targeting Lipid-Transfer Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pharmacology".

Deadline for manuscript submissions: closed (15 December 2022) | Viewed by 9458

Special Issue Editor

Dr. Bruno Mesmin

E-Mail Website
Guest Editor
Université Côte d’Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France
Interests: lipid-transfer proteins; membrane contact sites; cholesterol traffic; phosphoinositides; organelles; in vitro reconstitutions

Special Issue Information

Dear Colleagues,

Inter-organelle trafficking of membrane lipids is largely mediated by lipid transfer proteins (LTPs). These proteins possess domains with hydrophobic cavities that stabilize lipids and enable their transport between membranes across the aqueous phase of the cytosol. Besides the structural description of many LTPs, considerable progress has been made in our understanding of their functions at the molecular, cellular and physiological levels. It is clear that LTPs play a fundamental role in membrane biogenesis and signaling, and their malfunction can contribute to several diseases. In recent years, the development of pharmacology that specifically inhibits LTPs has shed new light on their mechanism of action and their importance in different pathophysiological contexts. One of the key issues is whether targeting LTPs with small molecules inhibitors will offer a promising route for potential treatments, such as for cancers, pathogen infections or metabolic disorders. A better understanding of how these different drugs act at the molecular and cellular levels will be essential to foster the development of effective therapies.

Dr. Bruno Mesmin
Guest Editor

Manuscript Submission Information

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Keywords

  • Lipid-transfer proteins
  • Small molecules inhibitors
  • Intracellular lipid transport
  • Membranes
  • Cancer
  • Infectious diseases
  • Membrane contact sites
  • Lipid metabolism

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Published Papers (3 papers)

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Review

21 pages, 3456 KiB  
Review
Non-Vesicular Lipid Transport Machinery in Leishmania donovani: Functional Implications in Host-Parasite Interaction
by Koushik Das and Tomoyoshi Nozaki
Int. J. Mol. Sci. 2023, 24(13), 10637; https://doi.org/10.3390/ijms241310637 - 26 Jun 2023
Cited by 1 | Viewed by 2534
Abstract
Eukaryotic cells have distinct membrane-enclosed organelles, each with a unique biochemical signature and specialized function. The unique identity of each organelle is greatly governed by the asymmetric distribution and regulated intracellular movement of two important biomolecules, lipids, and proteins. Non-vesicular lipid transport mediated [...] Read more.
Eukaryotic cells have distinct membrane-enclosed organelles, each with a unique biochemical signature and specialized function. The unique identity of each organelle is greatly governed by the asymmetric distribution and regulated intracellular movement of two important biomolecules, lipids, and proteins. Non-vesicular lipid transport mediated by lipid-transfer proteins (LTPs) plays essential roles in intra-cellular lipid trafficking and cellular lipid homeostasis, while vesicular transport regulates protein trafficking. A comparative analysis of non-vesicular lipid transport machinery in protists could enhance our understanding of parasitism and basis of eukaryotic evolution. Leishmania donovani, the trypanosomatid parasite, greatly depends on receptor-ligand mediated signalling pathways for cellular differentiation, nutrient uptake, secretion of virulence factors, and pathogenesis. Lipids, despite being important signalling molecules, have intracellular transport mechanisms that are largely unexplored in L. donovani. We have identified a repertoire of sixteen (16) potential lipid transfer protein (LTP) homologs based on a domain-based search on TriTrypDB coupled with bioinformatics analyses, which signifies the presence of well-organized lipid transport machinery in this parasite. We emphasized here their evolutionary uniqueness and conservation and discussed their potential implications for parasite biology with regards to future therapeutic targets against visceral leishmaniasis. Full article
(This article belongs to the Special Issue New Perspectives on Drugs Targeting Lipid-Transfer Proteins)
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20 pages, 2041 KiB  
Review
Natural Ligand-Mimetic and Nonmimetic Inhibitors of the Ceramide Transport Protein CERT
by Kentaro Hanada, Shota Sakai and Keigo Kumagai
Int. J. Mol. Sci. 2022, 23(4), 2098; https://doi.org/10.3390/ijms23042098 - 14 Feb 2022
Cited by 4 | Viewed by 2723
Abstract
Lipid transfer proteins (LTPs) are recognized as key players in the inter-organelle trafficking of lipids and are rapidly gaining attention as a novel molecular target for medicinal products. In mammalian cells, ceramide is newly synthesized in the endoplasmic reticulum (ER) and converted to [...] Read more.
Lipid transfer proteins (LTPs) are recognized as key players in the inter-organelle trafficking of lipids and are rapidly gaining attention as a novel molecular target for medicinal products. In mammalian cells, ceramide is newly synthesized in the endoplasmic reticulum (ER) and converted to sphingomyelin in the trans-Golgi regions. The ceramide transport protein CERT, a typical LTP, mediates the ER-to-Golgi transport of ceramide at an ER-distal Golgi membrane contact zone. About 20 years ago, a potent inhibitor of CERT, named (1R,3S)-HPA-12, was found by coincidence among ceramide analogs. Since then, various ceramide-resembling compounds have been found to act as CERT inhibitors. Nevertheless, the inevitable issue remains that natural ligand-mimetic compounds might directly bind both to the desired target and to various undesired targets that share the same natural ligand. To resolve this issue, a ceramide-unrelated compound named E16A, or (1S,2R)-HPCB-5, that potently inhibits the function of CERT has recently been developed, employing a series of in silico docking simulations, efficient chemical synthesis, quantitative affinity analysis, protein–ligand co-crystallography, and various in vivo assays. (1R,3S)-HPA-12 and E16A together provide a robust tool to discriminate on-target effects on CERT from off-target effects. This short review article will describe the history of the development of (1R,3S)-HPA-12 and E16A, summarize other CERT inhibitors, and discuss their possible applications. Full article
(This article belongs to the Special Issue New Perspectives on Drugs Targeting Lipid-Transfer Proteins)
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Graphical abstract

26 pages, 7654 KiB  
Review
Emerging Prospects for Combating Fungal Infections by Targeting Phosphatidylinositol Transfer Proteins
by Danish Khan, Aaron H. Nile, Ashutosh Tripathi and Vytas A. Bankaitis
Int. J. Mol. Sci. 2021, 22(13), 6754; https://doi.org/10.3390/ijms22136754 - 23 Jun 2021
Cited by 6 | Viewed by 3347
Abstract
The emergence of fungal “superbugs” resistant to the limited cohort of anti-fungal agents available to clinicians is eroding our ability to effectively treat infections by these virulent pathogens. As the threat of fungal infection is escalating worldwide, this dwindling response capacity is fueling [...] Read more.
The emergence of fungal “superbugs” resistant to the limited cohort of anti-fungal agents available to clinicians is eroding our ability to effectively treat infections by these virulent pathogens. As the threat of fungal infection is escalating worldwide, this dwindling response capacity is fueling concerns of impending global health emergencies. These developments underscore the urgent need for new classes of anti-fungal drugs and, therefore, the identification of new targets. Phosphoinositide signaling does not immediately appear to offer attractive targets due to its evolutionary conservation across the Eukaryota. However, recent evidence argues otherwise. Herein, we discuss the evidence identifying Sec14-like phosphatidylinositol transfer proteins (PITPs) as unexplored portals through which phosphoinositide signaling in virulent fungi can be chemically disrupted with exquisite selectivity. Recent identification of lead compounds that target fungal Sec14 proteins, derived from several distinct chemical scaffolds, reveals exciting inroads into the rational design of next generation Sec14 inhibitors. Development of appropriately refined next generation Sec14-directed inhibitors promises to expand the chemical weaponry available for deployment in the shifting field of engagement between fungal pathogens and their human hosts. Full article
(This article belongs to the Special Issue New Perspectives on Drugs Targeting Lipid-Transfer Proteins)
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