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Applied and Translational Research on Bioactive Peptides and Proteins
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Applied and Translational Research on Bioactive Peptides and Proteins

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

Deadline for manuscript submissions: 31 May 2024 | Viewed by 1648

Special Issue Editor

Dr. Paola Gagni

E-Mail Website
Guest Editor
Istituto di Scienze e Tecnologie Chimiche (SCITEC) “Giulio Natta”, Consiglio Nazionale delle Ricerche (CNR), 20133 Milan, Italy
Interests: biomarker discovery; extracellular vesicles; biosensors; microanalytical systems; protein/peptide microarrays; bioactive peptides; single-molecule detection; biotechnology

Special Issue Information

Dear Colleagues,

In the last two decades, the research on bioactive proteins and peptides has seen an exponential increase, mainly due to the advent of innovative and high-sensitivity detection platforms and due to advancements in molecular biology and biotechnology.

Every synthesized protein and its specific post-translational modification can putatively act as a bioactive molecule, enabling the use of a wide range of biological materials as a peptide source, from bacterial-, animal- or plant-derived cell cultures to biofluids, and from food to microbial environments. Furthermore, these proteins and peptides could be exploited as potential disease biomarkers, as they have been largely investigated in relation to their 3D structure, cellular compartmentalization, interactions and functions, paving the way to the discovery of new physiological and pathological pathways in living organisms. In addition to this, improvements in molecular engineering, biotechnology and chemical synthesis have contributed to the development of both a new generation of biosensors and innovative biotechnological drugs, such as, for example, antimicrobic agents, antihypertensive compounds, antioxidants or blood-lipid-lowering active molecules. Last, but not least, bioactive proteins play an increasingly central role in the food industry due to their nutraceutical effect.

In this Special Issue, we aim to highlight new applications of bioactive proteins and peptides in physiopathology translational research, biochemistry, nanotechnology and the food industry, which can act as biomarkers, innovative biosensors and tools integrated onto microanalytical platforms.

Dr. Paola Gagni
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

  • bioactive proteins/peptides
  • applied/translational research
  • bioengineering
  • biosensors
  • biomarkers
  • biotechnology
  • biochemistry
  • nanotechnology
  • food industry

Published Papers (2 papers)

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Research

14 pages, 3586 KiB  
Article
Chemical Modifications to Enhance the Drug Properties of a VIP Receptor Antagonist (ANT) Peptide
by Christina Lester, Jian-Ming Li, Tenzin Passang, Yuou Wang, Edmund K. Waller and Simon B. Blakey
Int. J. Mol. Sci. 2024, 25(8), 4391; https://doi.org/10.3390/ijms25084391 - 16 Apr 2024
Viewed by 270
Abstract
Antagonist peptides (ANTs) of vasoactive intestinal polypeptide receptors (VIP-Rs) are shown to enhance T cell activation and proliferation in vitro, as well as improving T cell-dependent anti-tumor response in acute myeloid leukemia (AML) murine models. However, peptide therapeutics often suffer from poor metabolic [...] Read more.
Antagonist peptides (ANTs) of vasoactive intestinal polypeptide receptors (VIP-Rs) are shown to enhance T cell activation and proliferation in vitro, as well as improving T cell-dependent anti-tumor response in acute myeloid leukemia (AML) murine models. However, peptide therapeutics often suffer from poor metabolic stability and exhibit a short half-life/fast elimination in vivo. In this study, we describe efforts to enhance the drug properties of ANTs via chemical modifications. The lead antagonist (ANT308) is derivatized with the following modifications: N-terminus acetylation, peptide stapling, and PEGylation. Acetylated ANT308 exhibits diminished T cell activation in vitro, indicating that N-terminus conservation is critical for antagonist activity. The replacement of residues 13 and 17 with cysteine to accommodate a chemical staple results in diminished survival using the modified peptide to treat mice with AML. However, the incorporation of the constraint increases survival and reduces tumor burden relative to its unstapled counterpart. Notably, PEGylation has a significant positive effect, with fewer doses of PEGylated ANT308 needed to achieve comparable overall survival and tumor burden in leukemic mice dosed with the parenteral ANT308 peptide, suggesting that polyethylene glycol (PEG) incorporation enhances longevity, and thus the antagonist activity of ANT308. Full article
(This article belongs to the Special Issue Applied and Translational Research on Bioactive Peptides and Proteins)
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12 pages, 3557 KiB  
Article
Screening of Oral Potential Angiotensin-Converting Enzyme Inhibitory Peptides from Zizyphus jujuba Proteins Based on Gastrointestinal Digestion In Vivo
by Xinchang Gao, Chaoying Zhang, Ning Wang, Jin-Ming Lin, Yali Dang and Yufen Zhao
Int. J. Mol. Sci. 2023, 24(21), 15848; https://doi.org/10.3390/ijms242115848 - 31 Oct 2023
Viewed by 754
Abstract
Plant proteins are a good source of active peptides, which can exert physiological effects on the body. Predicting the possible activity of plant proteins and obtaining active peptides with oral potential are challenging. In this study, the potential activity of peptides from Zizyphus [...] Read more.
Plant proteins are a good source of active peptides, which can exert physiological effects on the body. Predicting the possible activity of plant proteins and obtaining active peptides with oral potential are challenging. In this study, the potential activity of peptides from Zizyphus jujuba proteins after in silico simulated gastrointestinal digestion was predicted using the BIOPEP-UWM™ database. The ACE-inhibitory activity needs to be further investigated. The actual peptides in mouse intestines after the oral administration of Zizyphus jujuba protein were collected and analyzed, 113 Zizyphus jujuba peptides were identified, and 3D-QSAR models of the ACE-inhibitory activity were created and validated using a training set (34 peptides) and a test set (12 peptides). Three peptides, RLPHV, TVKPGL and KALVAP, were screened using the 3D-QSAR model and were found to bind to the active sites of the ACE enzyme, and their IC50 values were determined. Their values were 6.01, 3.81, and 17.06 μM, respectively. The in vitro digestion stabilities of the RLPHV, TVKPGL, and KALVAP peptides were 82%, 90%, and 78%. This article provides an integrated method for studying bioactive peptides derived from plant proteins. Full article
(This article belongs to the Special Issue Applied and Translational Research on Bioactive Peptides and Proteins)
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