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Marine Drugs
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Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential
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Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (31 May 2021) | Viewed by 51917

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Prof. Dr. Tatiana V. Ovchinnikova

E-Mail Website
Guest Editor
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Interests: marine natural products; marine peptides; innate immunity; host defense peptides; molecular mechanisms of antimicrobial and anticancer activity; structure elucidation; structure-function relationship; bioengineering; drug design; peptide antibiotics; peptide anticancer agents; drug resistance; bioorganic chemistry; biotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This second edition of the Special Issue “Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential” aims to collect papers on up-to-date information regarding isolation, structural elucidation, functional characterization, and therapeutic potential evaluation of peptides isolated from marine organisms. Chemical synthesis and biotechnological production of marine peptides and their mimetics will also be a focus of this Special Issue. In addition, this Special Issue will publish new results arising from a peptidomic approach.

Marine peptides that are diverse in structure and function have been found in various phyla, and their number has dynamically grown in recent years. Some of them are evolutionary ancient molecular factors of innate immunity that play a key role in host defense. A plethora of biological activities, including antibacterial, antifungal, antiviral, cytotoxic, neurotoxic, anticoagulant, antifreeze, endotoxin-binding, and immune-modulating, make marine peptides an attractive molecular basis for the design of innovative antibiotics, anticancer drugs, analgetics, medicines for neurological disorders, etc.

24 Papers were accepted and included in the first issue, which we published as a Special Issue book (https://www.mdpi.com/books/pdfview/book/1742). Following the success of the first Special Issue, as Guest Editor, I invite researchers in the field to contribute to the second edition entitled "Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential".

Prof. Dr. Tatiana V. Ovchinnikova
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. Marine Drugs 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 2900 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

  • marine peptides
  • structure
  • function
  • chemical synthesis
  • biotechnological production
  • peptidomics
  • therapeutic potential
  • antibacterial
  • antifungal
  • antiviral
  • cytotoxic
  • neurotoxic
  • anticancer
  • anticoagulant
  • endotoxin-binding
  • host defense
  • innate immunity
  • toxins
  • peptide drugs

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Published Papers (11 papers)

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Editorial

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5 pages, 203 KiB  
Editorial
Marine Peptides: Structure, Bioactivities, and a New Hope for Therapeutic Application
by Tatiana V. Ovchinnikova
Mar. Drugs 2021, 19(8), 407; https://doi.org/10.3390/md19080407 - 23 Jul 2021
Cited by 6 | Viewed by 2737
Abstract
Over the last years, plethora of bioactive peptides have been isolated from organisms which live in sea water [...] Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)

Research

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14 pages, 874 KiB  
Article
Limited Benefit of Marine Protein Hydrolysate on Physical Function and Strength in Older Adults: A Randomized Controlled Trial
by Linda Kornstad Nygård, Ingunn Mundal, Lisbeth Dahl, Jūratė Šaltytė Benth and Anne Marie Mork Rokstad
Mar. Drugs 2021, 19(2), 62; https://doi.org/10.3390/md19020062 - 27 Jan 2021
Cited by 5 | Viewed by 3824
Abstract
Age-related muscle wasting can compromise functional abilities of the elderly. Protein intake stimulates muscle protein synthesis; however, ageing muscle is more resistant to stimuli. This double-blinded, randomized, controlled trial is one of the first registered studies to evaluate the effects of a supplement [...] Read more.
Age-related muscle wasting can compromise functional abilities of the elderly. Protein intake stimulates muscle protein synthesis; however, ageing muscle is more resistant to stimuli. This double-blinded, randomized, controlled trial is one of the first registered studies to evaluate the effects of a supplement of marine protein hydrolysate (MPH) on measures of physical function and strength. Eighty-six older adults received nutritional supplements containing 3 g of MPH or a placebo for up to 12 months. Short Physical Performance Battery (SPPB), grip strength and gait speed were measured, and dietary intake was registered at baseline, 6 months, and 12 months. No difference was found between the intervention and control groups in mean change in SPPB (independent sample t-test, p = 0.41) or regarding time trend in SPPB, grip strength, or gait speed (linear mixed model). The participants in our study were well functioning, causing a ceiling effect in SPPB. Further, they had sufficient protein intake and were physically active. Differences in physical function between those completing the intervention and the dropouts might also have created bias in the results. We recommend that future studies of MPH be carried out on a more frail or malnourished population. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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18 pages, 3011 KiB  
Article
Proteomic Analysis of the Venom of Jellyfishes Rhopilema esculentum and Sanderia malayensis
by Thomas C. N. Leung, Zhe Qu, Wenyan Nong, Jerome H. L. Hui and Sai Ming Ngai
Mar. Drugs 2020, 18(12), 655; https://doi.org/10.3390/md18120655 - 21 Dec 2020
Cited by 14 | Viewed by 4282
Abstract
Venomics, the study of biological venoms, could potentially provide a new source of therapeutic compounds, yet information on the venoms from marine organisms, including cnidarians (sea anemones, corals, and jellyfish), is limited. This study identified the putative toxins of two species of jellyfish—edible [...] Read more.
Venomics, the study of biological venoms, could potentially provide a new source of therapeutic compounds, yet information on the venoms from marine organisms, including cnidarians (sea anemones, corals, and jellyfish), is limited. This study identified the putative toxins of two species of jellyfish—edible jellyfish Rhopilema esculentum Kishinouye, 1891, also known as flame jellyfish, and Amuska jellyfish Sanderia malayensis Goette, 1886. Utilizing nano-flow liquid chromatography tandem mass spectrometry (nLC–MS/MS), 3000 proteins were identified from the nematocysts in each of the above two jellyfish species. Forty and fifty-one putative toxins were identified in R. esculentum and S. malayensis, respectively, which were further classified into eight toxin families according to their predicted functions. Amongst the identified putative toxins, hemostasis-impairing toxins and proteases were found to be the most dominant members (>60%). The present study demonstrates the first proteomes of nematocysts from two jellyfish species with economic and environmental importance, and expands the foundation and understanding of cnidarian toxins. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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13 pages, 20805 KiB  
Article
Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator
by Ilia A. Krenev, Ekaterina S. Umnyakova, Igor E. Eliseev, Yaroslav A. Dubrovskii, Nikolay P. Gorbunov, Vladislav A. Pozolotin, Alexei S. Komlev, Pavel V. Panteleev, Sergey V. Balandin, Tatiana V. Ovchinnikova, Olga V. Shamova and Mikhail N. Berlov
Mar. Drugs 2020, 18(12), 631; https://doi.org/10.3390/md18120631 - 10 Dec 2020
Cited by 13 | Viewed by 3254
Abstract
Antimicrobial peptides (AMPs) are not only cytotoxic towards host pathogens or cancer cells but also are able to act as immunomodulators. It was shown that some human and non-human AMPs can interact with complement proteins and thereby modulate complement activity. Thus, AMPs could [...] Read more.
Antimicrobial peptides (AMPs) are not only cytotoxic towards host pathogens or cancer cells but also are able to act as immunomodulators. It was shown that some human and non-human AMPs can interact with complement proteins and thereby modulate complement activity. Thus, AMPs could be considered as the base for complement-targeted therapeutics development. Arenicins from the sea polychaete Arenicola marina, the classical example of peptides with a β-hairpin structure stabilized by a disulfide bond, were shown earlier to be among the most prospective regulators. Here, we investigate the link between arenicins’ structure and their antimicrobial, hemolytic and complement-modulating activities using the derivative Ar-1-(C/A) without a disulfide bond. Despite the absence of this bond, the peptide retains all important functional activities and also appears less hemolytic in comparison with the natural forms. These findings could help to investigate new complement drugs for regulation using arenicin derivatives. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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20 pages, 5856 KiB  
Article
Structure Elucidation and Functional Studies of a Novel β-hairpin Antimicrobial Peptide from the Marine Polychaeta Capitella teleta
by Pavel V. Panteleev, Andrey V. Tsarev, Victoria N. Safronova, Olesia V. Reznikova, Ilia A. Bolosov, Sergei V. Sychev, Zakhar O. Shenkarev and Tatiana V. Ovchinnikova
Mar. Drugs 2020, 18(12), 620; https://doi.org/10.3390/md18120620 - 4 Dec 2020
Cited by 20 | Viewed by 3470
Abstract
Endogenous antimicrobial peptides (AMPs) are evolutionary ancient molecular factors of innate immunity that play a key role in host defense. Among the most active and stable under physiological conditions AMPs are the peptides of animal origin that adopt a β-hairpin conformation stabilized by [...] Read more.
Endogenous antimicrobial peptides (AMPs) are evolutionary ancient molecular factors of innate immunity that play a key role in host defense. Among the most active and stable under physiological conditions AMPs are the peptides of animal origin that adopt a β-hairpin conformation stabilized by disulfide bridges. In this study, a novel BRICHOS-domain related AMP from the marine polychaeta Capitella teleta, named capitellacin, was produced as the recombinant analogue and investigated. The mature capitellacin exhibits high homology with the known β-hairpin AMP family—tachyplesins and polyphemusins from the horseshoe crabs. The β-hairpin structure of the recombinant capitellacin was proved by CD and NMR spectroscopy. In aqueous solution the peptide exists as monomeric right-handed twisted β-hairpin and its structure does not reveal significant amphipathicity. Moreover, the peptide retains this conformation in membrane environment and incorporates into lipid bilayer. Capitellacin exhibits a strong antimicrobial activity in vitro against a wide panel of bacteria including extensively drug-resistant strains. In contrast to other known β-hairpin AMPs, this peptide acts apparently via non-lytic mechanism at concentrations inhibiting bacterial growth. The molecular mechanism of the peptide antimicrobial action does not seem to be related to the inhibition of bacterial translation therefore other molecular targets may be assumed. The reduced cytotoxicity against human cells and high antibacterial cell selectivity as compared to tachyplesin-1 make it an attractive candidate compound for an anti-infective drug design. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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22 pages, 4036 KiB  
Article
Biological Activities of Cyclic and Acyclic B-Type Laxaphycins in SH-SY5Y Human Neuroblastoma Cells
by Rebeca Alvariño, Eva Alonso, Louis Bornancin, Isabelle Bonnard, Nicolas Inguimbert, Bernard Banaigs and Luis M. Botana
Mar. Drugs 2020, 18(7), 364; https://doi.org/10.3390/md18070364 - 15 Jul 2020
Cited by 17 | Viewed by 3735
Abstract
Laxaphycins are a family of non-ribosomal lipopeptides that have been isolated from several cyanobacteria. Some of these compounds have presented cytotoxic activities, but their mechanism of action is poorly understood. In this work, the already described laxaphycins B and B3, and acyclolaxaphycins B [...] Read more.
Laxaphycins are a family of non-ribosomal lipopeptides that have been isolated from several cyanobacteria. Some of these compounds have presented cytotoxic activities, but their mechanism of action is poorly understood. In this work, the already described laxaphycins B and B3, and acyclolaxaphycins B and B3 were isolated from the marine cyanobacteria Anabaena torulosa. Moreover, two new acyclic compounds, [des-(Ala4-Hle5)] acyclolaxaphycins B and B3, were purified from the herviborous gastropod Stylocheilus striatus, with this being the first description of biotransformed laxaphycins. The structure of these new compounds was elucidated, together with the absolute configuration of acyclolaxaphycins B and B3. The bioactivities of the six peptides were determined in SH-SY5Y human neuroblastoma cells. Laxaphycins B and B3 were cytotoxic (IC50: 1.8 and 0.8 µM, respectively) through the induction of apoptosis. In comparison, acyclic laxaphycins did not show cytotoxicity but affected mitochondrial functioning, so their effect on autophagy-related protein expression was analyzed, finding that acyclic peptides affected this process by increasing AMPK phosphorylation and inhibiting mTOR. This work confirms the pro-apoptotic properties of cyclic laxaphycins B and is the first report indicating the effects on autophagy of their acyclic analogs. Moreover, gastropod-derived compounds presented ring opening and amino-acids deletion, a biotransformation that had not been previously described. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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17 pages, 3279 KiB  
Article
Antioxidant Peptides from the Protein Hydrolysate of Spanish Mackerel (Scomberomorous niphonius) Muscle by in Vitro Gastrointestinal Digestion and Their In Vitro Activities
by Guo-Xu Zhao, Xiu-Rong Yang, Yu-Mei Wang, Yu-Qin Zhao, Chang-Feng Chi and Bin Wang
Mar. Drugs 2019, 17(9), 531; https://doi.org/10.3390/md17090531 - 12 Sep 2019
Cited by 32 | Viewed by 4051
Abstract
For the full use of Spanish mackerel (Scomberomorous niphonius) muscle to produce antioxidant peptides, the proteins of Spanish mackerel muscle were separately hydrolyzed under five kinds of enzymes and in vitro gastrointestinal digestion, and antioxidant peptides were isolated from the protein [...] Read more.
For the full use of Spanish mackerel (Scomberomorous niphonius) muscle to produce antioxidant peptides, the proteins of Spanish mackerel muscle were separately hydrolyzed under five kinds of enzymes and in vitro gastrointestinal digestion, and antioxidant peptides were isolated from the protein hydrolysate using ultrafiltration and multiple chromatography methods. The results showed that the hydrolysate (SMPH) prepared using in vitro GI digestion showed the highest degree of hydrolysis (27.45 ± 1.76%) and DPPH radical scavenging activity (52.58 ± 2.68%) at the concentration of 10 mg protein/mL among the six protein hydrolysates, and 12 peptides (SMP-1 to SMP-12) were prepared from SMPH. Among them, SMP-3, SMP-7, SMP-10, and SMP-11 showed the higher DPPH radical scavenging activities and were identified as Pro-Glu-Leu-Asp-Trp (PELDW), Trp-Pro-Asp-His-Trp (WPDHW), and Phe-Gly-Tyr-Asp-Trp-Trp (FGYDWW), and Tyr-Leu-His-Phe-Trp (YLHFW), respectively. PELDW, WPDHW, FGYDWW, and YLHFW showed high scavenging activities on DPPH radical (EC50 1.53, 0.70, 0.53, and 0.97 mg/mL, respectively), hydroxyl radical (EC50 1.12, 0.38, 0.26, and 0.67 mg/mL, respectively), and superoxide anion radical (EC50 0.85, 0.49, 0.34, and 1.37 mg/mL, respectively). Moreover, PELDW, WPDHW, FGYDWW, and YLHFW could dose-dependently inhibit lipid peroxidation in the linoleic acid model system and protect plasmid DNA (pBR322DNA) against oxidative damage induced by H2O2 in the tested model systems. In addition, PELDW, WPDHW, FGYDWW, and YLHFW could retain their high activities when they were treated under a low temperature (<60 °C) and a moderate pH environment (pH 5–9). These present results indicate that the protein hydrolysate, fractions, and isolated peptides from Spanish mackerel muscle have strong antioxidant activity and might have the potential to be used in health food products. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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Review

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30 pages, 7068 KiB  
Review
Marine Antitumor Peptide Dolastatin 10: Biological Activity, Structural Modification and Synthetic Chemistry
by Gang Gao, Yanbing Wang, Huiming Hua, Dahong Li and Chunlan Tang
Mar. Drugs 2021, 19(7), 363; https://doi.org/10.3390/md19070363 - 24 Jun 2021
Cited by 41 | Viewed by 6394
Abstract
Dolastatin 10 (Dol-10), a leading marine pentapeptide isolated from the Indian Ocean mollusk Dolabella auricularia, contains three unique amino acid residues. Dol-10 can effectively induce apoptosis of lung cancer cells and other tumor cells at nanomolar concentration, and it has been developed [...] Read more.
Dolastatin 10 (Dol-10), a leading marine pentapeptide isolated from the Indian Ocean mollusk Dolabella auricularia, contains three unique amino acid residues. Dol-10 can effectively induce apoptosis of lung cancer cells and other tumor cells at nanomolar concentration, and it has been developed into commercial drugs for treating some specific lymphomas, so it has received wide attention in recent years. In vitro experiments showed that Dol-10 and its derivatives were highly lethal to common tumor cells, such as L1210 leukemia cells (IC50 = 0.03 nM), small cell lung cancer NCI-H69 cells (IC50 = 0.059 nM), and human prostate cancer DU-145 cells (IC50 = 0.5 nM), etc. With the rise of antibody-drug conjugates (ADCs), milestone progress was made in clinical research based on Dol-10. A variety of ADCs constructed by combining MMAE or MMAF (Dol-10 derivatives) with a specific antibody not only ensured the antitumor activity of the drugs themself but also improved their tumor targeting and reduced the systemic toxicity. They are currently undergoing clinical trials or have been approved for marketing, such as Adcetris®, which had been approved for the treatment of anaplastic large T-cell systemic malignant lymphoma and Hodgkin lymphoma. Dol-10, as one of the most medically valuable natural compounds discovered up to now, has brought unprecedented hope for tumor treatment. It is particularly noteworthy that, by modifying the chemical structure of Dol-10 and combining with the application of ADCs technology, Dol-10 as a new drug candidate still has great potential for development. In this review, the biological activity and chemical work of Dol-10 in the advance of antitumor drugs in the last 35 years will be summarized, which will provide the support for pharmaceutical researchers interested in leading exploration of antitumor marine peptides. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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29 pages, 2323 KiB  
Review
Recent Advances in Small Peptides of Marine Origin in Cancer Therapy
by Qi-Ting Zhang, Ze-Dong Liu, Ze Wang, Tao Wang, Nan Wang, Ning Wang, Bin Zhang and Yu-Fen Zhao
Mar. Drugs 2021, 19(2), 115; https://doi.org/10.3390/md19020115 - 19 Feb 2021
Cited by 40 | Viewed by 4736
Abstract
Cancer is one of the leading causes of death in the world, and antineoplastic drug research continues to be a major field in medicine development. The marine milieu has thousands of biological species that are a valuable source of novel functional proteins and [...] Read more.
Cancer is one of the leading causes of death in the world, and antineoplastic drug research continues to be a major field in medicine development. The marine milieu has thousands of biological species that are a valuable source of novel functional proteins and peptides, which have been used in the treatment of many diseases, including cancer. In contrast with proteins and polypeptides, small peptides (with a molecular weight of less than 1000 Da) have overwhelming advantages, such as preferential and fast absorption, which can decrease the burden on human gastrointestinal function. Besides, these peptides are only connected by a few peptide bonds, and their small molecular weight makes it easy to modify and synthesize them. Specifically, small peptides can deliver nutrients and drugs to cells and tissues in the body. These characteristics make them stand out in relation to targeted drug therapy. Nowadays, the anticancer mechanisms of the small marine peptides are still largely not well understood; however, several marine peptides have been applied in preclinical treatment. This paper highlights the anticancer linear and cyclic small peptides in marine resources and presents a review of peptides and the derivatives and their mechanisms. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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21 pages, 1109 KiB  
Review
Marine Bioactive Peptides—An Overview of Generation, Structure and Application with a Focus on Food Sources
by Milica Pavlicevic, Elena Maestri and Marta Marmiroli
Mar. Drugs 2020, 18(8), 424; https://doi.org/10.3390/md18080424 - 13 Aug 2020
Cited by 48 | Viewed by 6880
Abstract
The biggest obstacles in the application of marine peptides are two-fold, as in the case of non-marine plant and animal-derived bioactive peptides: elucidating correlation between the peptide structure and its effect and demonstrating its stability in vivo. The structures of marine bioactive peptides [...] Read more.
The biggest obstacles in the application of marine peptides are two-fold, as in the case of non-marine plant and animal-derived bioactive peptides: elucidating correlation between the peptide structure and its effect and demonstrating its stability in vivo. The structures of marine bioactive peptides are highly variable and complex and dependent on the sources from which they are isolated. They can be cyclical, in the form of depsipeptides, and often contain secondary structures. Because of steric factors, marine-derived peptides can be resistant to proteolysis by gastrointestinal proteases, which presents an advantage over other peptide sources. Because of heterogeneity, amino acid sequences as well as preferred mechanisms of peptides showing specific bioactivities differ compared to their animal-derived counterparts. This review offers insights on the extreme diversity of bioactivities, effects, and structural features, analyzing 253 peptides, mainly from marine food sources. Similar to peptides in food of non-marine animal origin, a significant percentage (52.7%) of the examined sequences contain one or more proline residues, implying that proline might play a significant role in the stability of bioactive peptides. Additional problems with analyzing marine-derived bioactive peptides include their accessibility, extraction, and purification; this review considers the challenges and proposes possible solutions. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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24 pages, 2484 KiB  
Review
A Comprehensive Review of Bioactive Peptides from Marine Fungi and Their Biological Significance
by Fadia S. Youssef, Mohamed L. Ashour, Abdel Nasser B. Singab and Michael Wink
Mar. Drugs 2019, 17(10), 559; https://doi.org/10.3390/md17100559 - 29 Sep 2019
Cited by 84 | Viewed by 7287
Abstract
Fungal marine microorganisms are a valuable source of bioactive natural products. Fungal secondary metabolites mainly comprise alkaloids, terpenoids, peptides, polyketides, steroids, and lactones. Proteins and peptides from marine fungi show minimal human toxicity and less adverse effects comparable to synthetic drugs. This review [...] Read more.
Fungal marine microorganisms are a valuable source of bioactive natural products. Fungal secondary metabolites mainly comprise alkaloids, terpenoids, peptides, polyketides, steroids, and lactones. Proteins and peptides from marine fungi show minimal human toxicity and less adverse effects comparable to synthetic drugs. This review summarizes the chemistry and the biological activities of peptides that were isolated and structurally elucidated from marine fungi. Relevant fungal genera including Acremonium, Ascotricha, Aspergillus, Asteromyces, Ceratodictyon, Clonostachys, Emericella, Exserohilum, Microsporum, Metarrhizium, Penicillium, Scytalidium, Simplicillium, Stachylidium, Talaromyces, Trichoderma, as well as Zygosporium were extensively reviewed. About 131 peptides were reported from these 17 genera and their structures were unambiguously determined using 1D and 2D NMR (one and two dimensional nuclear magnetic resonance) techniques in addition to HRMS (high resolution mass spectrometry). Marfey and Mosher reactions were used to confirm the identity of these compounds. About 53% of the isolated peptides exhibited cytotoxic, antimicrobial, and antiviral activity, meanwhile, few of them showed antidiabetic, lipid lowering, and anti-inflammatory activity. However 47% of the isolated peptides showed no activity with respect to the examined biological activity and thus required further in depth biological assessment. In conclusion, when searching for bioactive natural products, it is worth exploring more peptides of fungal origin and assessing their biological activities. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides II: Structure, Function, and Therapeutic Potential)
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