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Biomolecules
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Active Peptides as Functional Biomolecules: In Vitro and In Vivo...
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Active Peptides as Functional Biomolecules: In Vitro and In Vivo Studies

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Natural and Bio-derived Molecules".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 14207

Special Issue Editors

Prof. Dr. Juei-Tang Cheng

E-Mail Website
Guest Editor
Department of Medical Research, Chi-Mei Medical Center, Tainan City 71004, Taiwan
Interests: metabolic disorders; insulin resistance; hepatokines; natural products; animal models
Special Issues, Collections and Topics in MDPI journals
Dr. Yumin Dai

E-Mail Website
Guest Editor
Department of Chemistry and Virginia Tech Center for Drug Discovery, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA
Interests: peptides; secondary metabolites; nutraceuticals; interactions between small molecules; enzymes; obesity; cytotoxicity; anti-HIV; analytical methods; LC-MS; NMR
Special Issues, Collections and Topics in MDPI journals
Dr. Marc Maresca

E-Mail Website1 Website2
Guest Editor
CNRS, Aix-Marseille University, Centrale Marseille, iSm2, 13013 Marseille, France
Interests: mycotoxins; fungal metabolites; antimicrobial; anticancer; antinflammatory; antioxidant
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Many chemical compounds have been developed and used in clinical practice. Active peptides, such as insulin, have been neglected, largely due to the difficulty of oral administration, which is associated with less absorption during application. Recently, a new insulin preparation that does not require injection has been successfully developed. Semaglutide, a peptide agonist of the GLP-1 receptor, can also now be taken orally. Therefore, the issue of peptide absorption appears to be less pressing. Notably, in addition to the role of incretins (GLP-1 and GIP) in metabolic homeosis, new research has focused on angiotensin (1–7) in the ACE2–Mas axis. Many active peptides must be developed as functional biomolecules in advance. Therefore, this Special Issue aims to publish the submissions for either in vitro or in vivo data on active peptides.

Prof. Dr. Juei-Tang Cheng
Dr. Yumin Dai
Dr. Marc Maresca
Guest Editors

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. Biomolecules is an international peer-reviewed open access monthly 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.

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Published Papers (3 papers)

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Research

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17 pages, 3974 KiB  
Article
Purification and Biological Properties of Raniseptins-3 and -6, Two Antimicrobial Peptides from Boana raniceps (Cope, 1862) Skin Secretion
by Gabriel Gonçalves de Freitas, João Martins Barbosa, Carlos José Correia de Santana, Ana Carolina Martins Magalhães, Keven Wender Rodrigues Macedo, Jéssica Oliveira de Souza, Jessica Schneider de Castro, Isadora Alves de Vasconcelos, Amanda Araújo Souza, Sonia Maria de Freitas, Sônia Nair Báo, Samuel Ribeiro Costa, Guilherme Dotto Brand, Ian de Meira Chaves, Vivian Vasconcelos Costa, Wagner Fontes, Osmindo Rodrigues Pires Júnior and Mariana S. Castro
Biomolecules 2023, 13(3), 576; https://doi.org/10.3390/biom13030576 - 22 Mar 2023
Cited by 3 | Viewed by 2348
Abstract
The number of multidrug-resistant pathogenic microorganisms has been growing in recent years, most of which is due to the inappropriate use of the commercial antibiotics that are currently available. The dissemination of antimicrobial resistance represents a serious global public health problem. Thus, it [...] Read more.
The number of multidrug-resistant pathogenic microorganisms has been growing in recent years, most of which is due to the inappropriate use of the commercial antibiotics that are currently available. The dissemination of antimicrobial resistance represents a serious global public health problem. Thus, it is necessary to search for and develop new drugs that can act as antimicrobial agents. Antimicrobial peptides are a promising alternative for the development of new therapeutic drugs. Anurans’ skin glands are a rich source of broad-spectrum antimicrobial compounds and hylids, a large and diverse family of tree frogs, are known as an important source of antimicrobial peptides. In the present study, two novel antimicrobial peptides, named Raniseptins-3 and -6, were isolated from Boana raniceps skin secretion and their structural and biological properties were evaluated. Raniseptins-3 and -6 are cationic, rich in hydrophobic residues, and adopt an α-helix conformation in the presence of SDS (35 mM). Both peptides are active against Gram-negative bacteria and Gram-positive pathogens, with low hemolytic activity at therapeutic concentrations. No activity was observed for yeasts, but the peptides are highly cytotoxic against B16F10 murine melanoma cells and NIH3T3 mouse fibroblast cells. None of the tested compounds showed improvement trends in the MTT and LDH parameters of MHV-3 infected cells at the concentrations tested. Full article
(This article belongs to the Special Issue Active Peptides as Functional Biomolecules: In Vitro and In Vivo Studies)
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20 pages, 4427 KiB  
Article
Design, Synthesis and Characterization of [G10a]-Temporin SHa Dendrimers as Dual Inhibitors of Cancer and Pathogenic Microbes
by Arif Iftikhar Khan, Shahzad Nazir, Aaqib Ullah, Muhammad Nadeem ul Haque, Rukesh Maharjan, Shabana U. Simjee, Hamza Olleik, Elise Courvoisier-Dezord, Marc Maresca and Farzana Shaheen
Biomolecules 2022, 12(6), 770; https://doi.org/10.3390/biom12060770 - 31 May 2022
Cited by 3 | Viewed by 2454
Abstract
As the technologies for peptide synthesis and development continue to mature, antimicrobial peptides (AMPs) are being widely studied as significant contributors in medicinal chemistry research. Furthermore, the advancement in the synthesis of dendrimers’ design makes dendrimers wonderful nanostructures with distinguishing properties. This study [...] Read more.
As the technologies for peptide synthesis and development continue to mature, antimicrobial peptides (AMPs) are being widely studied as significant contributors in medicinal chemistry research. Furthermore, the advancement in the synthesis of dendrimers’ design makes dendrimers wonderful nanostructures with distinguishing properties. This study foregrounds a temporin SHa analog, [G10a]-SHa, and its dendrimers as globular macromolecules possessing anticancer and antibacterial activities. These architectures of temporin SHa, named as [G10a]-SHa, its dendrimeric analogs [G10a]2-SHa and [G10a]3-SHa, and [G10a]2-SHa conjugated with a polymer molecule, i.e., Jeff-[G10a]2-SHa, were synthesized, purified on RP-HPLC and UPLC and fully characterized by mass, NMR spectroscopic techniques, circular dichroism, ultraviolet, infrared, dynamic light scattering, and atomic force microscopic studies. In pH- and temperature-dependent studies, all of the peptide dendrimers were found to be stable in the temperature range up to 40–60 °C and pH values in the range of 6–12. Biological-activity studies showed these peptide dendrimers possessed improved antibacterial activity against different strains of both Gram-positive and Gram-negative strains. Together, these dendrimers also possessed potent selective antiproliferative activity against human cancer cells originating from different organs (breast, lung, prostate, pancreas, and liver). The high hemolytic activity of [G10a]2-SHa and [G10a]3-SHa dendrimers, however, limits their use for topical treatment, such as in the case of skin infection. On the contrary, the antibacterial and anticancer activities of Jeff-[G10a]2-SHa, associated with its low hemolytic action, make it potentially suitable for systemic treatment. Full article
(This article belongs to the Special Issue Active Peptides as Functional Biomolecules: In Vitro and In Vivo Studies)
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Review

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37 pages, 11104 KiB  
Review
Exploring FDA-Approved Frontiers: Insights into Natural and Engineered Peptide Analogues in the GLP-1, GIP, GHRH, CCK, ACTH, and α-MSH Realms
by Othman Al Musaimi
Biomolecules 2024, 14(3), 264; https://doi.org/10.3390/biom14030264 - 22 Feb 2024
Cited by 7 | Viewed by 8435
Abstract
Peptides continue to gain significance in the pharmaceutical arena. Since the unveiling of insulin in 1921, the Food and Drug Administration (FDA) has authorised around 100 peptides for various applications. Peptides, although initially derived from endogenous sources, have evolved beyond their natural origins, [...] Read more.
Peptides continue to gain significance in the pharmaceutical arena. Since the unveiling of insulin in 1921, the Food and Drug Administration (FDA) has authorised around 100 peptides for various applications. Peptides, although initially derived from endogenous sources, have evolved beyond their natural origins, exhibiting favourable therapeutic effectiveness. Medicinal chemistry has played a pivotal role in synthesising valuable natural peptide analogues, providing synthetic alternatives with therapeutic potential. Furthermore, key chemical modifications have enhanced the stability of peptides and strengthened their interactions with therapeutic targets. For instance, selective modifications have extended their half-life and lessened the frequency of their administration while maintaining the desired therapeutic action. In this review, I analyse the FDA approval of natural peptides, as well as engineered peptides for diabetes treatment, growth-hormone-releasing hormone (GHRH), cholecystokinin (CCK), adrenocorticotropic hormone (ACTH), and α-melanocyte stimulating hormone (α-MSH) peptide analogues. Attention will be paid to the structure, mode of action, developmental journey, FDA authorisation, and the adverse effects of these peptides. Full article
(This article belongs to the Special Issue Active Peptides as Functional Biomolecules: In Vitro and In Vivo Studies)
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