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Molecules
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Chemical Modification of Functional Proteins for Diseases Detection and Treatment
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Chemical Modification of Functional Proteins for Diseases Detection and Treatment

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

Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 13002

Special Issue Editor

Dr. Clarence T. T. Wong

E-Mail Website
Guest Editor
Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Kowloon, Hong Kong
Interests: bioconjugation chemistry; peptide chemistry; drug delivery

Special Issue Information

Dear Colleagues,

In recent decades, chemical protein modification has become a blooming field of study. Driven by the rapid development of novel bioconjugation chemistry, researchers are now able to conjugate desired targets on many natural amino acids. State-of-the-art biorthogonal chemistries have further enhanced the site selectivity of protein modification, leading to the creation of new and remarkable functions on native proteins, the targeted delivery of functional proteins, the creation of unnatural post-translational modifications, and the assembly of multifunctional protein-based nanostructures and biopolymers that have been used in both in vitro and in vivo applications. With this vast array of invaluable tools, researchers can design and develop novel therapeutics that can be approved by the FDA and enter the market, such as PEGylated proteins and antibody–drug conjugates.

In this Special Issue, we will focus on the recently developed methodologies in the chemical modification of proteins, covering bioconjugation reactions, ligation chemistries, and bio-orthogonal chemistries that turn ordinary natural proteins into therapeutics. We will also highlight some of the novel examples and applications of these chemically modified proteins that were used in recent biomedical research. Researchers are welcome to contribute any work dedicated to the design, synthesis, and therapeutic evaluation of chemically modified proteins. 

Dr. Clarence T. T. Wong
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

  • chemical protein modification
  • protein conjugation
  • therapeutic proteins
  • drug–protein conjugate
  • protein probes
  • protein delivery

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Published Papers (2 papers)

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Research

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24 pages, 5066 KiB  
Article
Natural Plasmodium falciparum Infection Stimulates Human Antibodies to MSP1 Epitopes Identified in Mice Infection Models upon Non-Natural Modified Peptidomimetic Vaccination
by Zully Johana Rodríguez, Fredy Leonardo Melo, Angela Torres, Nikhil Agrawal, Jesús Alfredo Cortés-Vecino and José Manuel Lozano
Molecules 2023, 28(6), 2527; https://doi.org/10.3390/molecules28062527 - 10 Mar 2023
Cited by 1 | Viewed by 2026
Abstract
(1) Background: Malaria, a vector-borne infectious disease, is caused by parasites of the Plasmodium genus, responsible for increased extreme morbidity and mortality rates. Despite advances in approved vaccines, full protection has not yet been achieved upon vaccination, thus the development of more potent [...] Read more.
(1) Background: Malaria, a vector-borne infectious disease, is caused by parasites of the Plasmodium genus, responsible for increased extreme morbidity and mortality rates. Despite advances in approved vaccines, full protection has not yet been achieved upon vaccination, thus the development of more potent and safe immuno-stimulating agents for malaria prevention is a goal to be urgently accomplished. We have focused our research on a strategy to identify Plasmodium spp. epitopes by naturally acquired human antibodies and rodent malaria infection models immunized with site-directed non-natural antigens. (2) Methods: Some predictive algorithms and bioinformatics tools resembling different biological environments, such as phagosome-lysosome proteolytic degradation, affinity, and the high frequency of malaria-resistant and -sensitive HLA-II alleles were regarded for the proper selection of epitopes and potential testing. Each epitope’s binding profile to both host cells and HLA-II molecules was considered for such initial screening. (3) Results: Once selected, we define each epitope-peptide to be synthesized in terms of size and hydrophobicity, and introduced peptide-bond surrogates and non-natural amino acids in a site-directed fashion, and then they were produced by solid-phase peptide synthesis. Molecules were then tested by their antigenic and immunogenic properties compared to human sera from Colombian malaria-endemic areas. The antigenicity and protective capacity of each epitope-peptide in a rodent infection model were examined. The ability of vaccinated mice after being challenged with P. berghei ANKA and P. yoelii 17XL to control malaria led to the determination of an immune stimulation involving Th1 and Th1/Th2 mechanisms. In silico molecular dynamics and modeling provided some interactions insights, leading to possible explanations for protection due to immunization. (4) Conclusions: We have found evidence for proposing MSP1-modified epitopes to be considered as neutralizing antibody stimulators that are useful as probes for the detection of Plasmodium parasites, as well as for sub-unit components of a site-directed designed malaria vaccine candidate. Full article
(This article belongs to the Special Issue Chemical Modification of Functional Proteins for Diseases Detection and Treatment)
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Review

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32 pages, 9370 KiB  
Review
Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins
by Ajcharapan Tantipanjaporn and Man-Kin Wong
Molecules 2023, 28(3), 1083; https://doi.org/10.3390/molecules28031083 - 21 Jan 2023
Cited by 27 | Viewed by 10416
Abstract
The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and [...] Read more.
The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods. Full article
(This article belongs to the Special Issue Chemical Modification of Functional Proteins for Diseases Detection and Treatment)
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