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Natural and Un-Natural Peptides
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Natural and Un-Natural Peptides

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

Deadline for manuscript submissions: closed (30 June 2024) | Viewed by 2518

Special Issue Editor

Dr. Luca D. D'Andrea

E-Mail Website
Guest Editor
Istituto di Scienze e Tecnologie Chimiche “G. Natta”, CNR, Milan, Italy
Interests: bioorganic chemistry; peptide chemistry; peptide design; bioactive peptides; chemical ligation; protein chemical synthesis; bioconjugation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptides are biomolecules that are widespread in Nature, in all kingdoms of life, performing a myriad of functions— for example, acting as hormones or presenting antimicrobial activity as part of the organism’s defense system. Peptides are advantageous as they perform their activity with high selectivity and potency. Inspired by the features of natural peptides, researchers started to use un-natural peptides to modulate biological functions, and to develop novel drugs, materials or technological tools. To obtain these molecules or to understand their properties, peptides can be modified by introducing unnatural amino acids or modifications in the backbone/side chains. Linear and cyclic peptides can be obtained, and there is a growing interest in macrocyclic peptides for their pharmacological properties.

This Special Issue aims to collect contributions reporting exciting results on the synthesis, structural and functional characterization of natural peptides/peptidomimetics and their analogues, as well as un-natural peptides. Examples of fields of application include, but are not limited to, life and health sciences, chemical biology, biotechnological and material sciences. We are also interested in the discussion of innovative chemical strategies for peptide synthesis and modifications. We welcome all types of contribution covering the topic area, such as original research or review articles.

Dr. Luca D. D'Andrea
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

  • peptide chemistry
  • antimicrobial peptides
  • cell-penetrating peptides
  • peptides as drugs
  • peptides as diagnostics
  • peptide-based materials
  • bioactive peptides
  • antiviral peptides
  • anticancer peptides
  • immunogenic peptides
  • RiPPs
  • nonribosomal peptides

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Published Papers (2 papers)

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Research

22 pages, 3718 KiB  
Article
Bioactive Properties of Enzymatic Gelatin Hydrolysates Based on In Silico, In Vitro, and In Vivo Studies
by Fenny Crista A. Panjaitan, Sin-Ting Shie, Sung Hoon Park, Tesalonika Sevi, Wen-Ling Ko, Rotimi E. Aluko and Yu-Wei Chang
Molecules 2024, 29(18), 4402; https://doi.org/10.3390/molecules29184402 - 16 Sep 2024
Viewed by 295
Abstract
This current study aims to analyze the potential bioactivities possessed by the enzymatic hydrolysates of commercial bovine, porcine, and tilapia gelatins using bioinformatics in combination with in vitro and in vivo studies. The hydrolysate with superior inhibition of angiotensin converting enzyme (ACE) activity [...] Read more.
This current study aims to analyze the potential bioactivities possessed by the enzymatic hydrolysates of commercial bovine, porcine, and tilapia gelatins using bioinformatics in combination with in vitro and in vivo studies. The hydrolysate with superior inhibition of angiotensin converting enzyme (ACE) activity was used to treat the D-galactose (DG)-induced amnesic mice. In silico digestion of the gelatins led to the identification of peptide sequences with potential antioxidant, ACE-inhibitory, and anti-amnestic properties. The results of in vitro digestion revealed that the <1 kDa peptide fraction of porcine gelatin hydrolysate obtained after 1 h digestion with papain (PP) (PP1, <1 kDa) potently inhibited ACE, acetylcholinesterase, and prolyl endopeptidase activities at 87.42%, 21.24%, and 48.07%, respectively. Administering the PP1 to DG-induced amnesic mice ameliorated the spatial cognitive impairment and Morris water maze learning abilities. The dentate area morphology in the PP1-treated mice was relatively similar to the control group. In addition, PP1 enhanced the antioxidant capacity in the DG-induced amnesic mice. This study suggests that PP1 could serve as a potential treatment tool against oxidative stress, hypertension, and neurodegenerative diseases. Full article
(This article belongs to the Special Issue Natural and Un-Natural Peptides)
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13 pages, 1333 KiB  
Article
Enhancement of hMSC In Vitro Proliferation by Surface Immobilization of a Heparin-Binding Peptide
by Maura Cimino, Paula Parreira, Victoria Leiro, Aureliana Sousa, Raquel M. Gonçalves, Cristina C. Barrias and M. Cristina L. Martins
Molecules 2023, 28(8), 3422; https://doi.org/10.3390/molecules28083422 - 13 Apr 2023
Cited by 3 | Viewed by 1642
Abstract
The use of human Mesenchymal Stem Cells (hMSC) as therapeutic agents for advanced clinical therapies relies on their in vitro expansion. Over the last years, several efforts have been made to optimize hMSC culture protocols, namely by mimicking the cell physiological microenvironment, which [...] Read more.
The use of human Mesenchymal Stem Cells (hMSC) as therapeutic agents for advanced clinical therapies relies on their in vitro expansion. Over the last years, several efforts have been made to optimize hMSC culture protocols, namely by mimicking the cell physiological microenvironment, which strongly relies on signals provided by the extracellular matrix (ECM). ECM glycosaminoglycans, such as heparan-sulfate, sequester adhesive proteins and soluble growth factors at the cell membrane, orchestrating signaling pathways that control cell proliferation. Surfaces exposing the synthetic polypeptide poly(L-lysine, L-leucine) (pKL) have previously been shown to bind heparin from human plasma in a selective and concentration-dependent manner. To evaluate its effect on hMSC expansion, pKL was immobilized onto self-assembled monolayers (SAMs). The pKL-SAMs were able to bind heparin, fibronectin and other serum proteins, as demonstrated by quartz crystal microbalance with dissipation (QCM-D) studies. hMSC adhesion and proliferation were significantly increased in pKL-SAMs compared to controls, most probably related to increased heparin and fibronectin binding to pKL surfaces. This proof-of-concept study highlights the potential of pKL surfaces to improve hMSC in vitro expansion possible through selective heparin/serum protein binding at the cell-material interface. Full article
(This article belongs to the Special Issue Natural and Un-Natural Peptides)
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