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Molecules
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Drug Design and Activity Screening of Targeted Proteins
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Drug Design and Activity Screening of Targeted Proteins

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".

Deadline for manuscript submissions: 31 May 2024 | Viewed by 3160

Special Issue Editor

Prof. Dr. Dan Liu

E-Mail Website
Guest Editor
Key Laboratory of Structure-based Drug Design and Discovery, Ministry of Education, Shenyang Pharmaceutical University, Shenyang, China
Interests: drug design and synthesis; antitumor activity evaluation; structure– activity relationships; structure-based drug design; ligand-based drug design; drug metabolism

Special Issue Information

Dear Colleagues,

Protein is the most basic structural and functional material of organisms, and it participates in almost all life activities. Its abnormal function is the cause of many major diseases, such as cancer, cardiovascular and cerebrovascular diseases, and so on. As the main target of drug action, proteins include enzymes, receptors, ion channels, and other types. With the development of biochemistry, molecular biology, proteomics, and AI technology, a large number of protein spatial structures have been resolved, making it possible to design drugs targeting these proteins. Directly activating or inhibiting its function, regulating its function through the bypass, or promoting its degradation can make drugs targeting proteins have good therapeutic effects. In this Special Issue of Molecules, entitled “Drug Design and Activity Screening of Targeted Proteins”, I invite manuscript submissions that focus on agents having potential for the treatment of diseases and conditions affecting human and animal health. Original research articles or reviews that discuss the design, synthesis, activities, and mode of action of drug candidates targeting precise protein are particularly welcome.

Prof. Dr. Dan Liu
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. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). 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

  • drug design and synthesis
  • structure-based drug design
  • medicinal chemistry
  • innovative drug research
  • action between drug and target
  • docking research

Published Papers (2 papers)

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Research

13 pages, 2777 KiB  
Article
Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst—A Structural and Functional Analysis
by Gabriel Žoldák, Thomas A. Knappe, Anne-Juliane Geitner, Christian Scholz, Holger Dobbek, Franz X. Schmid and Roman P. Jakob
Molecules 2024, 29(7), 1440; https://doi.org/10.3390/molecules29071440 - 23 Mar 2024
Viewed by 516
Abstract
Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low, but it could be [...] Read more.
Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low, but it could be increased by inserting the chaperone domain from the homolog SlyD of E. coli near the prolyl isomerase active site. We inserted two other chaperone domains into human FKBP12: the chaperone domain of SlpA from E. coli, and the chaperone domain of SlyD from Thermococcus sp. Both stabilized FKBP12 and greatly increased its folding activity. The insertion of these chaperone domains had no influence on the FKBP12 and the chaperone domain structure, as revealed by two crystal structures of the chimeric proteins. The relative domain orientations differ in the two crystal structures, presumably representing snapshots of a more open and a more closed conformation. Together with crystal structures from SlyD-like proteins, they suggest a path for how substrate proteins might be transferred from the chaperone domain to the prolyl isomerase domain. Full article
(This article belongs to the Special Issue Drug Design and Activity Screening of Targeted Proteins)
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17 pages, 2978 KiB  
Article
Activation-Free Sulfonyl Fluoride Probes for Fragment Screening
by László Petri, Péter Ábrányi-Balogh, Noémi Csorba, Aaron Keeley, József Simon, Ivan Ranđelović, József Tóvári, Gitta Schlosser, Dániel Szabó, László Drahos and György M. Keserű
Molecules 2023, 28(7), 3042; https://doi.org/10.3390/molecules28073042 - 29 Mar 2023
Cited by 4 | Viewed by 2243
Abstract
SuFEx chemistry is based on the unique reactivity of the sulfonyl fluoride group with a range of nucleophiles. Accordingly, sulfonyl fluorides label multiple nucleophilic amino acid residues, making these reagents popular in both chemical biology and medicinal chemistry applications. The reactivity of sulfonyl [...] Read more.
SuFEx chemistry is based on the unique reactivity of the sulfonyl fluoride group with a range of nucleophiles. Accordingly, sulfonyl fluorides label multiple nucleophilic amino acid residues, making these reagents popular in both chemical biology and medicinal chemistry applications. The reactivity of sulfonyl fluorides nominates this warhead chemotype as a candidate for an external, activation-free general labelling tag. Here, we report the synthesis and characterization of a small sulfonyl fluoride library that yielded the 3-carboxybenzenesulfonyl fluoride warhead for tagging tractable targets at nucleophilic residues. Based on these results, we propose that coupling diverse fragments to this warhead would result in a library of sulfonyl fluoride bits (SuFBits), available for screening against protein targets. SuFBits will label the target if it binds to the core fragment, which facilitates the identification of weak fragments by mass spectrometry. Full article
(This article belongs to the Special Issue Drug Design and Activity Screening of Targeted Proteins)
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