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Special Issue "Peptide Chemistry Ⅱ"

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

Deadline for manuscript submissions: 30 June 2019

Special Issue Editor

Guest Editor
Prof. Dr. Wojciech Kamysz, Pharm. D.

Department of Inorganic Chemistry, Faculty of Pharmacy, Medical University of Gdansk, Hallera 107, 80-416 Gdansk, Poland
Website | E-Mail
Interests: peptide synthesis; peptide design; antimicrobial peptides; pro-ecological methods of analysis and purification of chemical compounds

Special Issue Information

Dear Colleagues,

Peptides are compounds with a veriety of biolgical properties that offer multiple applications. Since 1963, when solid-phase peptide synthesis (SPPS) was introduced by Merriefield, a great deal of effort has been expended on the development of this method. The biomedical applications of peptides are somewhat limited, due to their poor oral bioavibility, chemical instability, or low membrane permeability. However, thanks to the efforts of many scientific groups, many peptides are currently under clinical trials and some have been registered as drugs.

In view of the recent developments, research articles covering all areas of peptide chemistry are welcome for publication in this Special Issue of Molecules.

Prof. Wojciech Kamysz, Pharm. D.
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 papers will be 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 1800 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

  • Solid-phase peptide synthesis
  • Peptide coupling agents
  • Bioactive peptides
  • Lipopeptides
  • Cyclic peptides
  • Peptide-based biomaterials
  • Peptidomimetics
  • Self-assembly
  • Anaysis of peptides
  • Peptide chromatography

Published Papers (3 papers)

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Research

Open AccessArticle
The Limitations of Collagen/CPP Hybrid Peptides as Carriers for Cancer Drugs to FaDu Cells
Molecules 2019, 24(4), 676; https://doi.org/10.3390/molecules24040676
Received: 30 December 2018 / Revised: 7 February 2019 / Accepted: 12 February 2019 / Published: 14 February 2019
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Abstract
The in vitro efficacy of cancer prodrugs varies significantly between malignant cell lines. The most commonly identified problems relate to delivery: uptake mechanism, endosomal entrapment, and drug release. Here we present the study of collagen/cell penetrating hybrid (COL/CPP) peptide carriers intended to deliver [...] Read more.
The in vitro efficacy of cancer prodrugs varies significantly between malignant cell lines. The most commonly identified problems relate to delivery: uptake mechanism, endosomal entrapment, and drug release. Here we present the study of collagen/cell penetrating hybrid (COL/CPP) peptide carriers intended to deliver paclitaxel to the hypopharyngeal carcinoma (FaDu) cells. Confocal microscopy imaging revealed the surprising response of FaDu cell to COL/CPP in comparison to previously studied cancer cell lines: hybrid peptides that carry both COL and CPP domain adsorb on the FaDu cell surface. While the CPP domain was design to facilitate the cellular uptake, in the case of FaDu cells, it also induced detrimental interactions with the cell membrane. Despite surface adsorption, the colocalization study with endosomal markers EEA1 and LAMP1 reveals that COL/CPP is internalized via endosomal pathway, peptides are able to escape before lysosome formation and release paclitaxel. Therefore, the main obstacle for paclitaxel delivery to FaDu cells appears to be related to cell surface properties. This behavior seems specific to FaDu cells, and could be linked to previously reported overexpression of T5, heparanase splice variants that produces protein lacking enzymatic activity of heparanase. This results in increased concentration of HSPG on FaDu cell surface, and possibly creates a barrier for cellular uptake of highly charged COL/CPP. Full article
(This article belongs to the Special Issue Peptide Chemistry Ⅱ)
Figures

Figure 1

Open AccessArticle
In Silico Analysis of Bioactive Peptides Released from Giant Grouper (Epinephelus lanceolatus) Roe Proteins Identified by Proteomics Approach
Molecules 2018, 23(11), 2910; https://doi.org/10.3390/molecules23112910
Received: 14 October 2018 / Revised: 1 November 2018 / Accepted: 6 November 2018 / Published: 8 November 2018
PDF Full-text (1707 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were [...] Read more.
Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were characterized through compiled proteomics techniques (SDS-PAGE, in-gel digestion, mass spectrometry and on-line Mascot database analysis). These proteins were subjected to in silico analysis using BLAST and BIOPEP-UWM database. Sequence similarity search by BLAST revealed that the aligned vitellogenin sequences from Epinephelus coioides and Epinephelus lanceolatus share 70% identity, which indicates that the sequence sample has significant similarity with proteins in sequence databases. Moreover, prediction of potential bioactivities through BIOPEP-UWM database resulted in high numbers of peptides predominantly with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE-I) inhibitory activities. Pepsin (pH > 2) was predicted to be the most promising enzyme for the production of bioactive peptides from GR protein, which theoretically released 82 DPP-IV inhibitory peptides and 47 ACE-I inhibitory peptides. Overall, this work highlighted the potentiality of giant grouper roe as raw material for the generation of pharmaceutical products. Furthermore, the application of proteomics and in silico techniques provided rapid identification of proteins and useful prediction of its potential bioactivities. Full article
(This article belongs to the Special Issue Peptide Chemistry Ⅱ)
Figures

Graphical abstract

Open AccessArticle
The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage
Molecules 2018, 23(10), 2618; https://doi.org/10.3390/molecules23102618
Received: 13 September 2018 / Revised: 6 October 2018 / Accepted: 9 October 2018 / Published: 12 October 2018
PDF Full-text (2051 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
This study aimed to investigate the variation of molecular functional properties of peanut protein isolate (PPI) over the storage process and reveal the correlation between the PPI secondary structure and properties in the storage procedure. After storage, the molecular properties of PPI changed [...] Read more.
This study aimed to investigate the variation of molecular functional properties of peanut protein isolate (PPI) over the storage process and reveal the correlation between the PPI secondary structure and properties in the storage procedure. After storage, the molecular properties of PPI changed significantly (p < 0.05). Extending storage time resulted in a decrease in free sulfhydryl content, fluorescence intensity, surface hydrophobicity and emulsifying properties, which was accompanied by an increase in protein particle size. The results of infrared spectroscopy suggested the content decline of α-helix and β-sheet, and the content rise of β-turn and random coil. Based on bivariate correlation analysis, it was revealed that surface hydrophobicity and emulsifying activity of PPI was significantly affected by α-helix and by β-turn (p < 0.05), respectively. This research supplied more information for the relationship between the peanut protein’s secondary structure and functional properties over the stored process. Full article
(This article belongs to the Special Issue Peptide Chemistry Ⅱ)
Figures

Graphical abstract

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