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Special Issue "Peptides for Health Benefits 2019"

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

Deadline for manuscript submissions: 30 September 2019.

Special Issue Editors

Guest Editor
Dr. Blanca Hernández-Ledesma

Instituto de Investigación en Ciencias de la Alimentación (CIAL), Consejo Superior de Investigaciones Científicas (CSIC). Nicolás Cabrera 9, Madrid 28049, Spain
Website | E-Mail
Interests: bioactive peptides; chemoprevention; antioxidant activity; food proteins; bioavailability
Guest Editor
Dr. Cristina Martínez-Villaluenga

Institute of Food Science, Technology and Nutrition (ICTAN), Spanish National Research Council (CSIC), Jose Antonio Novais 10, 28040 Madrid, Spain
Website | E-Mail
Interests: germination; grains; nutritional value; bioactivity, bioactive compounds

Special Issue Information

Dear Colleagues,

In recent years, peptides have received increased interest by the pharmaceutical industry. The high potency, specificity and good safety profile are the main strengths of bioactive peptides as new and promising therapies that may fill the gap between small molecules and protein drugs. These positive attributes of peptides, along with advances in drug delivery technologies, have afforded a renewed interest in the discovery, optimization and development of peptides as pharmacological therapy. Among bioactive peptides, those released from food protein sources have acquired importance as nutraceutical and active components in functional foods because they are known to possess regulatory functions that can lead to health benefits.

This Special Issue, “Peptides for Health Benefits”, will cover a selection of recent research papers, reviews, short communications, as well as perspectives in the field of bioactive peptides. It aims to cover all aspects of peptide research in relation to health promotion. In particular, this Special Issue emphasizes current knowledge and research trends concerning bioactive peptides, including identification and quantification of peptides from new sources, methods for their production and purification, structure-function relationships, mechanisms of action, development of novel in vitro and in vivo assays for the evaluation of their bioactivity, physiological evidence to support health benefits, and peptide stability, bioavailability, and sensory (or techno-functional) properties. Papers regarding the development of new drugs, functional foods or nutraceuticals based on bioactive peptides will be also taken into consideration.

Dr. Blanca Hernández-Ledesma
Dr. Cristina Martínez-Villaluenga
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 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. 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

  • Human health
  • Bioactive peptides
  • Food peptides
  • Biological activity
  • Peptidomics
  • In vitro and in vivo assays
  • Identification and characterization
  • Functional foods
  • Peptide-based therapies

Related Special Issue

Published Papers (10 papers)

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Research

Jump to: Review

Open AccessArticle
Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity
Int. J. Mol. Sci. 2019, 20(16), 3931; https://doi.org/10.3390/ijms20163931
Received: 5 July 2019 / Revised: 23 July 2019 / Accepted: 29 July 2019 / Published: 13 August 2019
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Abstract
The extraction and enzymatic hydrolysis of collagen from sheepskins at different times of hydrolysis (0, 10, 15, 20, 30 min, 1, 2, 3 and 4 h) were investigated in terms of amino acid content (hydroxyproline), isoelectric point, molecular weight (Mw) by sodium dodecyl [...] Read more.
The extraction and enzymatic hydrolysis of collagen from sheepskins at different times of hydrolysis (0, 10, 15, 20, 30 min, 1, 2, 3 and 4 h) were investigated in terms of amino acid content (hydroxyproline), isoelectric point, molecular weight (Mw) by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method, viscosity, Fourier-transform infrared (FTIR) spectroscopy, antioxidant capacity by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays, thermal properties (Differential Scanning Calorimetry) and morphology by scanning electron microscopy (SEM) technique. The kinetics of hydrolysis showed an increase in the protein and hydroxyproline concentration as the hydrolysis time increased to 4 h. FTIR spectra allowed us to identify the functional groups of hydrolysed collagen (HC) in the amide I region for collagen. The isoelectric point shifted to lower values compared to the native collagen precursor. The change in molecular weight and viscosity from time 0 min to 4 h promoted important antioxidant activity in the resulting HC. The lower the Mw, the greater the ability to donate an electron or hydrogen to stabilize radicals. From the SEM images it was evident that HC after 2 h had a porous and spongy structure. These results suggest that HC could be a good alternative to replace HC from typical sources like pigs, cows and fish. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Graphical abstract

Open AccessArticle
Osteostatin Inhibits Collagen-Induced Arthritis by Regulation of Immune Activation, Pro-Inflammatory Cytokines, and Osteoclastogenesis
Int. J. Mol. Sci. 2019, 20(16), 3845; https://doi.org/10.3390/ijms20163845
Received: 26 July 2019 / Revised: 4 August 2019 / Accepted: 5 August 2019 / Published: 7 August 2019
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Abstract
In chronic inflammatory joint diseases, such as rheumatoid arthritis, there is an important bone loss. Parathyroid hormone-related protein (PTHrP) and related peptides have shown osteoinductive properties in bone regeneration models, but there are no data on inflammatory joint destruction. We have investigated whether [...] Read more.
In chronic inflammatory joint diseases, such as rheumatoid arthritis, there is an important bone loss. Parathyroid hormone-related protein (PTHrP) and related peptides have shown osteoinductive properties in bone regeneration models, but there are no data on inflammatory joint destruction. We have investigated whether the PTHrP (107-111) C-terminal peptide (osteostatin) could control the development of collagen-induced arthritis in mice. Administration of osteostatin (80 or 120 μg/kg s.c.) after the onset of disease decreased the severity of arthritis as well as cartilage and bone degradation. This peptide reduced serum IgG2a levels as well as T cell activation, with the downregulation of RORγt+CD4+ T cells and upregulation of FoxP3+CD8+ T cells in lymph nodes. The levels of key cytokines, such as interleukin(IL)-1β, IL-2, IL-6, IL-17, and tumor necrosis factor-α in mice paws were decreased by osteostatin treatment, whereas IL-10 was enhanced. Bone protection was related to reductions in receptor activator of nuclear factor-κB ligand, Dickkopf-related protein 1, and joint osteoclast area. Osteostatin improves arthritis and controls bone loss by inhibiting immune activation, pro-inflammatory cytokines, and osteoclastogenesis. Our results support the interest of osteostatin for the treatment of inflammatory joint conditions. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Intragenic Antimicrobial Peptide Hs02 Hampers the Proliferation of Single- and Dual-Species Biofilms of P. aeruginosa and S. aureus: A Promising Agent for Mitigation of Biofilm-Associated Infections
Int. J. Mol. Sci. 2019, 20(14), 3604; https://doi.org/10.3390/ijms20143604
Received: 17 June 2019 / Revised: 12 July 2019 / Accepted: 15 July 2019 / Published: 23 July 2019
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Abstract
Pseudomonas aeruginosa and Staphylococcus aureus are two major pathogens involved in a large variety of infections. Their co-occurrence in the same site of infection has been frequently reported and is linked to enhanced virulence and difficulty of treatment. Herein, the antimicrobial and antibiofilm [...] Read more.
Pseudomonas aeruginosa and Staphylococcus aureus are two major pathogens involved in a large variety of infections. Their co-occurrence in the same site of infection has been frequently reported and is linked to enhanced virulence and difficulty of treatment. Herein, the antimicrobial and antibiofilm activities of an intragenic antimicrobial peptide (IAP), named Hs02, which was uncovered from the human unconventional myosin 1H protein, were investigated against several P. aeruginosa and S. aureus strains, including multidrug-resistant (MDR) isolates. The antibiofilm activity was evaluated on single- and dual-species biofilms of P. aeruginosa and S. aureus. Moreover, the effect of peptide Hs02 on the membrane fluidity of the strains was assessed through Laurdan generalized polarization (GP). Minimum inhibitory concentration (MIC) values of peptide Hs02 ranged from 2 to 16 μg/mL against all strains and MDR isolates. Though Hs02 was not able to hamper biofilm formation by some strains at sub-MIC values, it clearly affected 24 h preformed biofilms, especially by reducing the viability of the bacterial cells within the single- and dual-species biofilms, as shown by confocal laser scanning microscopy (CLSM) and atomic force microscopy (AFM) images. Laurdan GP values showed that Hs02 induces membrane rigidification in both P. aeruginosa and S. aureus. Peptide Hs02 can potentially be a lead for further improvement as an antibiofilm agent. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Alterations in Galanin-Like Immunoreactivity in the Enteric Nervous System of the Porcine Stomach Following Acrylamide Supplementation
Int. J. Mol. Sci. 2019, 20(13), 3345; https://doi.org/10.3390/ijms20133345
Received: 31 May 2019 / Revised: 1 July 2019 / Accepted: 4 July 2019 / Published: 8 July 2019
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Abstract
In recent years, a significant increase in the consumption of products containing large amounts of acrylamide (e.g., chips, fries, coffee), especially among young people has been noted. The present study was created to establish the impact of acrylamide supplementation, in tolerable daily intake [...] Read more.
In recent years, a significant increase in the consumption of products containing large amounts of acrylamide (e.g., chips, fries, coffee), especially among young people has been noted. The present study was created to establish the impact of acrylamide supplementation, in tolerable daily intake (TDI) dose and a dose ten times higher than TDI, on the population of galanin-like immunoreactive (GAL-LI) stomach neurons in pigs. Additionally, in the present study, the possible functional co-operation of GAL with other neuroactive substances and their role in acrylamide intoxication was investigated. Using double-labelling immunohistochemistry, alterations in the expression of GAL were examined in the porcine stomach enteric neurons after low and high doses of acrylamide supplementation. Generally, upregulation in GAL-LI immunoreactivity in both myenteric and submucous plexuses was noted in all stomach fragments studied. Additionally, the proportion of GAL-expressing cell bodies simultaneously immunoreactive to vasoactive intestinal peptide (VIP), neuronal nitric oxide synthase (nNOS) and cocaine- and amphetamine- regulated transcript peptide (CART) also increased. The results suggest neurotrophic or/and neuroprotective properties of GAL and possible co-operation of GAL with VIP, nNOS, CART in the recovery processes in the stomach enteric nervous system (ENS) neurons following acrylamide intoxication. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
EDB-FN Targeted Peptide–Drug Conjugates for Use against Prostate Cancer
Int. J. Mol. Sci. 2019, 20(13), 3291; https://doi.org/10.3390/ijms20133291
Received: 30 May 2019 / Revised: 24 June 2019 / Accepted: 28 June 2019 / Published: 4 July 2019
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Abstract
Prostate cancer (PCa) is the most common malignancy in men and is the leading cause of cancer-related male mortality. A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that [...] Read more.
Prostate cancer (PCa) is the most common malignancy in men and is the leading cause of cancer-related male mortality. A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that can differentiate aggressive PCa from benign prostatic hyperplasia. We synthesized and optimized the stability of ligand 1 by amide cyclization to obtain [KTVRTSADE] 8 using Fmoc/tBu solid-phase chemistry. Optimized targeting ligand 8 was found to be stable in phosphate buffered saline (PBS, pH 6.5, 7.0, and 7.5) and under redox conditions, with a half-life longer than 8 h. Confocal microscopy studies demonstrated increased binding of ligand 8 to EDB-FN compared to ligand 1. Therefore, we hypothesized that the EDB-FN targeted peptides (1 and 8) conjugated with an anticancer drug via a hydrolyzable linker would provide selective cytotoxicity to the cancer cells. To test our hypothesis, we selected both the normal prostate cell line, RWPE-1, and the cancerous prostate cell lines, PC3, DU-145, LNCaP, and C4-2, to evaluate the anticancer activity of synthesized peptide–drug conjugates. Docetaxel (Doce) and doxorubicin (Dox) were used as anticancer drugs. Dox conjugate 13 containing disulfide linkage showed comparable cytotoxicity versus Dox after 72 h incubation in all the cancer cell lines, whereas it was found to be less cytotoxic on RWPE-1, suggesting that it can act as a Dox prodrug. Doce conjugate 14 was found to be less cytotoxic in all the cell lines as compared to drug alone. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors
Int. J. Mol. Sci. 2019, 20(10), 2482; https://doi.org/10.3390/ijms20102482
Received: 8 April 2019 / Revised: 23 April 2019 / Accepted: 15 May 2019 / Published: 20 May 2019
Cited by 1 | PDF Full-text (1327 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown [...] Read more.
Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study
Int. J. Mol. Sci. 2019, 20(9), 2274; https://doi.org/10.3390/ijms20092274
Received: 10 April 2019 / Revised: 3 May 2019 / Accepted: 6 May 2019 / Published: 8 May 2019
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Abstract
Human apolipoprotein E (apoE) is a major component of lipoprotein particles, and under physiological conditions, is involved in plasma cholesterol transport. Human apolipoprotein E found in three isoforms (E2; E3; E4) is a member of a family of apolipoproteins that under pathological conditions [...] Read more.
Human apolipoprotein E (apoE) is a major component of lipoprotein particles, and under physiological conditions, is involved in plasma cholesterol transport. Human apolipoprotein E found in three isoforms (E2; E3; E4) is a member of a family of apolipoproteins that under pathological conditions are detected in extracellular amyloid depositions in several amyloidoses. Interestingly, the lipid-free apoE form has been shown to be co-localized with the amyloidogenic Aβ peptide in amyloid plaques in Alzheimer’s disease, whereas in particular, the apoE4 isoform is a crucial risk factor for late-onset Alzheimer’s disease. Evidence at the experimental level proves that apoE self-assembles into amyloid fibrilsin vitro, although the misfolding mechanism has not been clarified yet. Here, we explored the mechanistic insights of apoE misfolding by testing short apoE stretches predicted as amyloidogenic determinants by AMYLPRED, and we computationally investigated the dynamics of apoE and an apoE–Αβ complex. Our in vitro biophysical results prove that apoE peptide–analogues may act as the driving force needed to trigger apoE aggregation and are supported by the computational apoE outcome. Additional computational work concerning the apoE–Αβ complex also designates apoE amyloidogenic regions as important binding sites for oligomeric Αβ; taking an important step forward in the field of Alzheimer’s anti-aggregation drug development. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Prediction of Bioactive Peptides from Chlorella sorokiniana Proteins Using Proteomic Techniques in Combination with Bioinformatics Analyses
Int. J. Mol. Sci. 2019, 20(7), 1786; https://doi.org/10.3390/ijms20071786
Received: 20 February 2019 / Revised: 3 April 2019 / Accepted: 9 April 2019 / Published: 11 April 2019
Cited by 2 | PDF Full-text (2323 KB) | HTML Full-text | XML Full-text
Abstract
Chlorella is one of the most nutritionally important microalgae with high protein content and can be a good source of potential bioactive peptides. In the current study, isolated proteins from Chlorella sorokiniana were subjected to in silico analysis to predict potential peptides with [...] Read more.
Chlorella is one of the most nutritionally important microalgae with high protein content and can be a good source of potential bioactive peptides. In the current study, isolated proteins from Chlorella sorokiniana were subjected to in silico analysis to predict potential peptides with biological activities. Molecular characteristics of proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and proteomics techniques. A total of eight proteins were identified by proteomics techniques from 10 protein bands of the SDS-PAGE. The predictive result by BIOPEP’s profile of bioactive peptides tools suggested that proteins of C. sorokiniana have the highest number of dipeptidyl peptidase-IV (DPP IV) inhibitors, with high occurrence of other bioactive peptides such as angiotensin-I converting enzyme (ACE) inhibitor, glucose uptake stimulant, antioxidant, regulating, anti-amnestic and antithrombotic peptides. In silico analysis of enzymatic hydrolysis revealed that pepsin (pH > 2), bromelain and papain were proteases that can release relatively larger quantity of bioactive peptides. In addition, combinations of different enzymes in hydrolysis were observed to dispense higher numbers of bioactive peptides from proteins compared to using individual proteases. Results suggest the potential of protein isolated from C. sorokiniana could be a source of high value products with pharmaceutical and nutraceutical application potential. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Open AccessArticle
Development of a Soy Protein Hydrolysate with an Antihypertensive Effect
Int. J. Mol. Sci. 2019, 20(6), 1496; https://doi.org/10.3390/ijms20061496
Received: 15 February 2019 / Revised: 12 March 2019 / Accepted: 21 March 2019 / Published: 25 March 2019
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Abstract
In this study, we combined enzymatic hydrolysis and lactic acid fermentation to generate an antihypertensive product. Soybean protein isolates were first hydrolyzed by Prozyme and subsequently fermented with Lactobacillus rhamnosus EBD1. After fermentation, the in vitro angiotensin-converting enzyme (ACE) inhibitory activity of the [...] Read more.
In this study, we combined enzymatic hydrolysis and lactic acid fermentation to generate an antihypertensive product. Soybean protein isolates were first hydrolyzed by Prozyme and subsequently fermented with Lactobacillus rhamnosus EBD1. After fermentation, the in vitro angiotensin-converting enzyme (ACE) inhibitory activity of the product (P-SPI) increased from 60.8 ± 2.0% to 88.24 ± 3.2%, while captopril (a positive control) had an inhibitory activity of 94.20 ± 5.4%. Mass spectrometry revealed the presence of three potent and abundant ACE inhibitory peptides, PPNNNPASPSFSSSS, GPKALPII, and IIRCTGC in P-SPI. Hydrolyzing P-SPI with gastrointestinal proteases did not significantly affect its ACE inhibitory ability. Also, oral administration of P-SPI (200 mg/kg body weight) to spontaneous hypertensive rats (SHRs) for 6 weeks significantly lowered systolic blood pressure (−19 ± 4 mm Hg, p < 0.05) and controlled body weight gain relative to control SHRs that were fed with physiological saline. Overall, P-SPI could be used as an antihypertensive functional food. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)
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Review

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Open AccessReview
Chemotactic Ligands that Activate G-Protein-Coupled Formylpeptide Receptors
Int. J. Mol. Sci. 2019, 20(14), 3426; https://doi.org/10.3390/ijms20143426
Received: 19 June 2019 / Revised: 3 July 2019 / Accepted: 5 July 2019 / Published: 12 July 2019
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Abstract
Leukocyte infiltration is a hallmark of inflammatory responses. This process depends on the bacterial and host tissue-derived chemotactic factors interacting with G-protein-coupled seven-transmembrane receptors (GPCRs) expressed on the cell surface. Formylpeptide receptors (FPRs in human and Fprs in mice) belong to the family [...] Read more.
Leukocyte infiltration is a hallmark of inflammatory responses. This process depends on the bacterial and host tissue-derived chemotactic factors interacting with G-protein-coupled seven-transmembrane receptors (GPCRs) expressed on the cell surface. Formylpeptide receptors (FPRs in human and Fprs in mice) belong to the family of chemoattractant GPCRs that are critical mediators of myeloid cell trafficking in microbial infection, inflammation, immune responses and cancer progression. Both murine Fprs and human FPRs participate in many patho-physiological processes due to their expression on a variety of cell types in addition to myeloid cells. FPR contribution to numerous pathologies is in part due to its capacity to interact with a plethora of structurally diverse chemotactic ligands. One of the murine Fpr members, Fpr2, and its endogenous agonist peptide, Cathelicidin-related antimicrobial peptide (CRAMP), control normal mouse colon epithelial growth, repair and protection against inflammation-associated tumorigenesis. Recent developments in FPR (Fpr) and ligand studies have greatly expanded the scope of these receptors and ligands in host homeostasis and disease conditions, therefore helping to establish these molecules as potential targets for therapeutic intervention. Full article
(This article belongs to the Special Issue Peptides for Health Benefits 2019)

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Meat proteins as dipeptidyl peptidase IV inhibitors for the management of type 2 diabetes mellitus (T2DM) – in silico study

Author: Joanna Stadnik et al.

Title: Identification of antimicrobial peptides in fresh and insect meal from Gromphadorhina portentosa

Author: Agata Józefiak et al.

Title: Pathogen- and host-derived chemotactic peptides that activate  G-protein-coupled formylpeptide receptors

Author: Ji Ming Wang et al.

Title: The human tripeptide GHK induces strong anti-cancer gene expression in human breast cancer MCF7 and prostate cancer PC3 cells

Author: Anna Margolina et al.

Title: the bactericidal activity of temporin analogues against S. aureus MRSA

Author: Joanna Koziel et al.

Title: HCMV infection, neuronal migration, and schizophrenia: a peptide connection

Author: Guglielmo Lucchese et al.

Title: Anti-sepsis effect of Ps-K18 derived from Pseduin-2: Inhibitory effect by antibacterial and anti-inflammatory activity.

Author: Yangmee Kim er al.

Title: How oxygen availability affects the antimicrobial efficacy of host defense peptides: Lessons learned from studying the copper-binding peptides piscidins 1 and 3

Author: Myriam Cotton et al.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
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