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Pharmaceutical Nanoimaging and Nanoengineering
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Special Issue "Pharmaceutical Nanoimaging and Nanoengineering"

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

Deadline for manuscript submissions: 29 February 2024 | Viewed by 474

Special Issue Editor

Prof. Dr. Yuri Lyubchenko

E-Mail Website
Guest Editor
Department of Pharmaceutical Sciences, College of Pharmacy, WSH, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA
Interests: nanomedicine; biophysics; DNA replication and recombination; protein-DNA interaction; chromatin structure and dynamics; Alzheimer's disease; Parkinson's disease; amyloid protein aggregation; protein misfolding; alpha-synuclein; beta amyloid; protein–protein interaction; computational modeling; nanoimaging; single-molecule biophysics; force spectroscopy; atomic force microscopy; AFM
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Iof IJMS invites significant contributions on imaging and probing at a nanoscale along with nfocused on the study, development and refinement of materials at a very small scale. Papers dealing with nanomaterials and how they can lead to novel medicinal approaches are very welcome. Topics of interest include, but are not limited to, the following:

  • Nanoimaging of biomolecules including AFM, STM, optical tweezers and other single-molecule biophysics approaches.
  • Structure and dynamics of biomolecular systems at the nanoscale.
  • Design of nanoassemblies.
  • Interaction of nanoassemblies with cells and organs.
  • Nanotechnology in drug design and delivery.
  • Liposomes, micells, polymer–drug conjugate and other carriers for nanomedicine.
  • Antibody–drug conjugates.

Prof. Dr. Yuri Lyubchenko
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • AFM
  • optical tweezers
  • magnetic tweezers
  • single-molecule fluorescence
  • protein self-assembly
  • nanomedicine
  • ion channels
  • drug delivery

Published Papers (1 paper)

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Research

22 pages, 2781 KiB  
Article
Drug-Induced Conformational Dynamics of P-Glycoprotein Underlies the Transport of Camptothecin Analogs
by
Gershon A. K. Mensah
,
Katherine G. Schaefer
,
Michael G. Bartlett
,
Arthur G. Roberts
and
Gavin M. King
Int. J. Mol. Sci. 2023, 24(22), 16058; https://doi.org/10.3390/ijms242216058 - 07 Nov 2023
Viewed by 374
Abstract
P-glycoprotein (Pgp) plays a pivotal role in drug bioavailability and multi-drug resistance development. Understanding the protein’s activity and designing effective drugs require insight into the mechanisms underlying Pgp-mediated transport of xenobiotics. In this study, we investigated the drug-induced conformational changes in Pgp and [...] Read more.
P-glycoprotein (Pgp) plays a pivotal role in drug bioavailability and multi-drug resistance development. Understanding the protein’s activity and designing effective drugs require insight into the mechanisms underlying Pgp-mediated transport of xenobiotics. In this study, we investigated the drug-induced conformational changes in Pgp and adopted a conformationally-gated model to elucidate the Pgp-mediated transport of camptothecin analogs (CPTs). While Pgp displays a wide range of conformations, we simplified it into three model states: ‘open-inward’, ‘open-outward’, and ‘intermediate’. Utilizing acrylamide quenching of Pgp fluorescence as a tool to examine the protein’s tertiary structure, we observed that topotecan (TPT), SN-38, and irinotecan (IRT) induced distinct conformational shifts in the protein. TPT caused a substantial shift akin to AMPPNP, suggesting ATP-independent ‘open-outward’ conformation. IRT and SN-38 had relatively moderate effects on the conformation of Pgp. Experimental atomic force microscopy (AFM) imaging supports these findings. Further, the rate of ATPase hydrolysis was correlated with ligand-induced Pgp conformational changes. We hypothesize that the separation between the nucleotide-binding domains (NBDs) creates a conformational barrier for substrate transport. Substrates that reduce the conformational barrier, like TPT, are better transported. The affinity for ATP extracted from Pgp-mediated ATP hydrolysis kinetics curves for TPT was about 2-fold and 3-fold higher than SN-38 and IRT, respectively. On the contrary, the dissociation constants (KD) determined by fluorescence quenching for these drugs were not significantly different. Saturation transfer double difference (STDD) NMR of TPT and IRT with Pgp revealed that similar functional groups of the CPTs are accountable for Pgp-CPTs interactions. Efforts aimed at modifying these functional groups, guided by available structure-activity relationship data for CPTs and DNA-Topoisomerase-I complexes, could pave the way for the development of more potent next-generation CPTs. Full article
(This article belongs to the Special Issue Pharmaceutical Nanoimaging and Nanoengineering)
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