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18 pages, 1965 KiB

Open AccessArticle

Biological Activity of Hydrophilic Extract of Chlorella vulgaris Grown on Post-Fermentation Leachate from a Biogas Plant Supplied with Stillage and Maize Silage

by Dariusz Zielinski, Justyna Fraczyk, Marcin Debowski, Marcin Zielinski, Zbigniew J. Kaminski, Dorota Kregiel, Claus Jacob and Beata Kolesinska

Molecules 2020, 25(8), 1790; https://doi.org/10.3390/molecules25081790 - 14 Apr 2020

Cited by 32 | Viewed by 4412

Abstract

Algae are employed commonly in cosmetics, food and pharmaceuticals, as well as in feed production and biorefinery processes. In this study, post-fermentation leachate from a biogas plant which exploits stillage and maize silage was utilized as a culture medium for Chlorella vulgaris. [...] Read more.

Algae are employed commonly in cosmetics, food and pharmaceuticals, as well as in feed production and biorefinery processes. In this study, post-fermentation leachate from a biogas plant which exploits stillage and maize silage was utilized as a culture medium for Chlorella vulgaris. The content of polyphenols in hydrophilic extracts of the Chlorella vulgaris biomass was determined, and the extracts were evaluated for their antioxidant activity (DPPH assay), antibacterial activity (against Escherichia coli, Lactobacillus plantarum, Staphylococcus aureus, Staphylococcus epidermidis) and antifungal activity (against Aspergillus niger, Candida albicans, Saccharomyces cerevisiae). The use of the post-fermentation leachate was not found to affect the biological activity of the microalgae. The aqueous extract of Chlorella vulgaris biomass was also observed to exhibit activity against nematodes. The results of this study suggest that Chlorella vulgaris biomass cultured on post-fermentation leachate from a biogas plant can be successfully employed as a source of natural antioxidants, food supplements, feed, natural antibacterial and antifungal compounds, as well as in natural methods of plant protection. Full article

(This article belongs to the Special Issue Peptide Chemistry Ⅱ)

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20 pages, 1307 KiB

Open AccessArticle

Ultrashort Cationic Lipopeptides–Effect of N-Terminal Amino Acid and Fatty Acid Type on Antimicrobial Activity and Hemolysis

by Damian Neubauer, Maciej Jaśkiewicz, Marta Bauer, Krzysztof Gołacki and Wojciech Kamysz

Molecules 2020, 25(2), 257; https://doi.org/10.3390/molecules25020257 - 8 Jan 2020

Cited by 33 | Viewed by 5244

Abstract

Ultrashort cationic lipopeptides (USCLs) are promising antimicrobial agents that hypothetically may be alternatively used to combat pathogens such as bacteria and fungi. In general, USCLs consist of fatty acid chains and a few basic amino acid residues. The main shortcoming of USCLs is [...] Read more.

Ultrashort cationic lipopeptides (USCLs) are promising antimicrobial agents that hypothetically may be alternatively used to combat pathogens such as bacteria and fungi. In general, USCLs consist of fatty acid chains and a few basic amino acid residues. The main shortcoming of USCLs is their relatively high cytotoxicity and hemolytic activity. This study focuses on the impact of the hydrophobic fatty acid chain, on both antimicrobial and hemolytic activities. To learn more about this region, a series of USCLs with different straight-chain fatty acids (C8, C10, C12, C14) attached to the tripeptide with two arginine residues were synthesized. The amino acid at the N-terminal position was exchanged for proteinogenic and non-proteinogenic amino acid residues (24 in total). Moreover, the branched fatty acid residues were conjugated to N-terminus of a dipeptide with two arginine residues. All USCLs had C-terminal amides. USCLs were tested against reference bacterial strains (including ESKAPE group) and Candida albicans. The hemolytic potential was tested on human erythrocytes. Hydrophobicity of the compounds was evaluated by RP-HPLC. Shortening of the fatty acid chain and simultaneous addition of amino acid residue at N-terminus were expected to result in more selective and active compounds than those of the reference lipopeptides with similar lipophilicity. Hypothetically, this approach would also be beneficial to other antimicrobial peptides where N-lipidation strategy was used to improve their biological characteristics. Full article

(This article belongs to the Special Issue Peptide Chemistry Ⅱ)

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10 pages, 3437 KiB

Open AccessFeature PaperArticle

Scope and Limitations of γ-Valerolactone (GVL) as a Green Solvent to be Used with Base for Fmoc Removal in Solid Phase Peptide Synthesis

by Ashish Kumar, Anamika Sharma, Beatriz G. de la Torre and Fernando Albericio

Molecules 2019, 24(21), 4004; https://doi.org/10.3390/molecules24214004 - 5 Nov 2019

Cited by 21 | Viewed by 5170

Abstract

GVL is a green solvent used in Fmoc-based solid-phase peptide synthesis. It is susceptible to ring opening in the presence of bases such as piperidines, which are used to remove the Fmoc protecting group. Here we studied the formation of the corresponding acyl [...] Read more.

GVL is a green solvent used in Fmoc-based solid-phase peptide synthesis. It is susceptible to ring opening in the presence of bases such as piperidines, which are used to remove the Fmoc protecting group. Here we studied the formation of the corresponding acyl piperidides by time-dependent monitoring using NMR. The results, corroborated by theoretical calculations, indicate that a solution of piperidines in GVL should be prepared daily for a better Fmoc removal. Full article

(This article belongs to the Special Issue Peptide Chemistry Ⅱ)

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22 pages, 4339 KiB

Open AccessArticle

Evaluating the Bioactivity of a Novel Antimicrobial and Anticancer Peptide, Dermaseptin-PS4(Der-PS4), from the Skin Secretion of Phyllomedusa sauvagii

by Dong Chen, Xiaowei Zhou, Xi Chen, Linyuan Huang, Xinping Xi, Chengbang Ma, Mei Zhou, Lei Wang and Tianbao Chen

Molecules 2019, 24(16), 2974; https://doi.org/10.3390/molecules24162974 - 16 Aug 2019

Cited by 23 | Viewed by 4281

Abstract

Dermaseptins belonging to a large family of cationic membrane-disruption antimicrobial peptides display extensive antibacterial and antiproliferative activities depending on a coil-to-helix transition and the specific structural parameters. Herein, a novel dermaseptin peptide named Der-PS4 was discovered from the skin secretion of the waxy [...] Read more.

Dermaseptins belonging to a large family of cationic membrane-disruption antimicrobial peptides display extensive antibacterial and antiproliferative activities depending on a coil-to-helix transition and the specific structural parameters. Herein, a novel dermaseptin peptide named Der-PS4 was discovered from the skin secretion of the waxy monkey tree frog, Phyllomedusa sauvagii. The complementary DNA (cDNA)-encoding precursor was obtained relying on “shotgun” cloning, and afterwards, a mature peptide amino acid sequence was identified by reverse-phase high performance liquid chromatography (RP-HPLC) and MS/MS. Specimens were chemically synthesized and applied for further functional studies. Structural analysis demonstrated a higher α-helical content in the membrane-mimetic environment compared with that in the ammonium acetate/water circumstance. Der-PS4 displayed a broad spectrum of antimicrobial activities against tested pathogenic microorganisms, however, exhibiting slight membrane-damaging effectiveness towards horse red blood cells. Coincident with the inhibitory activities on pathogens, Der-PS4 also showed considerable biofilm eradicating impact. Also, Der-PS4 penetrated cell membrane in a relative short period under each minimum bactericidal concentration. In addition, Der-PS4 possessed antiproliferative capacity against five cancer cell lines, while presenting slight suppressing effect on human microvascular endothelial, HMEC-1. These findings provide a promising insight for the discovery and development of novel drugs from a natural source. Full article

(This article belongs to the Special Issue Peptide Chemistry Ⅱ)

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13 pages, 2665 KiB

Open AccessArticle

The Limitations of Collagen/CPP Hybrid Peptides as Carriers for Cancer Drugs to FaDu Cells

by Kevin Ho, Cristobal Morfin and Katarzyna Slowinska

Molecules 2019, 24(4), 676; https://doi.org/10.3390/molecules24040676 - 14 Feb 2019

Cited by 3 | Viewed by 3457

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)

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15 pages, 1707 KiB

Open AccessArticle

In Silico Analysis of Bioactive Peptides Released from Giant Grouper (Epinephelus lanceolatus) Roe Proteins Identified by Proteomics Approach

by Fenny Crista A. Panjaitan, Honey Lyn R. Gomez and Yu-Wei Chang

Molecules 2018, 23(11), 2910; https://doi.org/10.3390/molecules23112910 - 8 Nov 2018

Cited by 39 | Viewed by 5401

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)

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14 pages, 2051 KiB

Open AccessArticle

The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage

by Xiaotong Sun, Hua Jin, Yangyang Li, Haiying Feng, Chunhong Liu and Jing Xu

Molecules 2018, 23(10), 2618; https://doi.org/10.3390/molecules23102618 - 12 Oct 2018

Cited by 19 | Viewed by 3297

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)

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Review

Jump to: Research

18 pages, 1383 KiB

Open AccessReview

Application of QCM in Peptide and Protein-Based Drug Product Development

by Dorian Migoń, Tomasz Wasilewski and Dariusz Suchy

Molecules 2020, 25(17), 3950; https://doi.org/10.3390/molecules25173950 - 29 Aug 2020

Cited by 44 | Viewed by 6816

Abstract

AT-cut quartz crystals vibrating in the thickness-shear mode (TSM), especially quartz crystal resonators (QCRs), are well known as very efficient mass sensitive systems because of their sensitivity, accuracy, and biofunctionalization capacity. They are highly reliable in the measurement of the mass of deposited [...] Read more.

AT-cut quartz crystals vibrating in the thickness-shear mode (TSM), especially quartz crystal resonators (QCRs), are well known as very efficient mass sensitive systems because of their sensitivity, accuracy, and biofunctionalization capacity. They are highly reliable in the measurement of the mass of deposited samples, in both gas and liquid matrices. Moreover, they offer real-time monitoring, as well as relatively low production and operation costs. These features make mass sensitive systems applicable in a wide range of different applications, including studies on protein and peptide primary packaging, formulation, and drug product manufacturing process development. This review summarizes the information on some particular implementations of quartz crystal microbalance (QCM) instruments in protein and peptide drug product development as well as their future prospects. Full article

(This article belongs to the Special Issue Peptide Chemistry Ⅱ)

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