Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Kurpe, Stanislav R.; Grishin, Sergei Y.; Surin, Alexey K.; Panfilov, Alexander; Slizen, M V; Chowdhury, Saikat Dutta; Galzitskaya, Oxana V.

doi:10.3390/ijms21249552

Cited by 49 publications

(41 citation statements)

References 290 publications

(197 reference statements)

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“…Coaggregation of peptide and S1 protein was tested for 2 S1 proteins and 5 peptides: S1 T. thermophilus with V10T, R23T, R23I ( Kurpe et al, 2020 ; Supplementary Table S1 ), and S1 P. aeruginosa with R23R, and R23L at a ratio of 1:5 (0.5 mg/ml and 2.5 mg/ml) (see Supplementary Table S1 ). In all these cases, the co-aggregation led to the formation of aggregates of different sizes and fibrils of different diameters.…”

Section: Amyloidogenicity Of Peptides and Formation Of Fibrilsmentioning

confidence: 99%

“…It should be noted that among antimicrobial drugs, only seven peptide antibiotics were approved for use, and of more than 10,000 antimicrobial peptides (AMPs), only 61 are at the stage of preclinical and clinical trials ( Koo and Seo, 2019 ), which demonstrates the complexity of the development and implementation of new antimicrobial substances. One of the possible solutions to combat pathogenic microorganisms is the development and use of new antimicrobial peptides (AMP) ( Kurpe et al, 2020 ; Lee et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

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Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs

Galzitskaya

2021

Front. Mol. Biosci.

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Antimicrobial peptides (AMPs) and similar compounds are potential candidates for combating antibiotic-resistant bacteria. The hypothesis of directed co-aggregation of the target protein and an amyloidogenic peptide acting as an antimicrobial peptide was successfully tested for peptides synthesized on the basis of ribosomal S1 protein in the bacterial culture of T. thermophilus. Co-aggregation of the target protein and amyloidogenic peptide was also tested for the pathogenic ribosomal S1 protein from P. aeruginosa. Almost all peptides that we selected as AMPs, prone to aggregation and formation of fibrils, based on the amino acid sequence of ribosomal S1 protein from E. coli, T. thermophilus, P. aeruginosa, formed amyloid fibrils. We have demonstrated that amyloidogenic peptides are not only toxic to their target cells, but also some of them have antimicrobial activity. Controlling the aggregation of vital bacterial proteins can become one of the new directions of research and form the basis for the search and development of targeted antibacterial drugs.

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Section: Amyloidogenicity Of Peptides and Formation Of Fibrilsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs

Galzitskaya

2021

Front. Mol. Biosci.

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“…Natural AMPs have potent and broad-spectrum activity against multiple classes of bacteria, yeasts, fungi, viruses and parasites ( Huan et al, 2020 ; Luong et al, 2020 ), displaying bacteriostatic, microbicidal and cytolytic properties ( Pasupuleti et al, 2012 ). Moreover, the interest in AMPs has recently increased during the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) pandemic in the search of new antiviral molecules to counteract COVID-19 disease ( Kurpe et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields

Moretta

Scieuzo

Petrone

et al. 2021

Front. Cell. Infect. Microbiol.

313

198

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Antibiotics are essential drugs used to treat pathogenic bacteria, but their prolonged use contributes to the development and spread of drug-resistant microorganisms. Antibiotic resistance is a serious challenge and has led to the need for new alternative molecules less prone to bacterial resistance. Antimicrobial peptides (AMPs) have aroused great interest as potential next-generation antibiotics, since they are bioactive small proteins, naturally produced by all living organisms, and representing the first line of defense against fungi, viruses and bacteria. AMPs are commonly classified according to their sources, which are represented by microorganisms, plants and animals, as well as to their secondary structure, their biosynthesis and their mechanism of action. They find application in different fields such as agriculture, food industry and medicine, on which we focused our attention in this review. Particularly, we examined AMP potential applicability in wound healing, skin infections and metabolic syndrome, considering their ability to act as potential Angiotensin-Converting Enzyme I and pancreatic lipase inhibitory peptides as well as antioxidant peptides. Moreover, we argued about the pharmacokinetic and pharmacodynamic approaches to develop new antibiotics, the drug development strategies and the formulation approaches which need to be taken into account in developing clinically suitable AMP applications.

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“…The other strategy is to screen antiviral candidates from the naturally occurring bioactive peptides. In this aspect, antimicrobial peptides (AMPs) are attracting increasing attention with regard to their possibility of blocking cellular surface receptors and/or disruption of virus cell membrane at the stage of virus entry [ 9 , 10 , 11 , 12 , 13 , 14 ]. As the effectors of the innate immune system of multicellular organisms, AMPs establish the first−line defense towards microbial infection and are being exploited as alternatives of conventional anti−infective agents to combat bacterial and fungal infections [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

A Fungal Defensin Targets the SARS−CoV−2 Spike Receptor−Binding Domain

Gao

Zhu

2021

JoF

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Coronavirus Disease 2019 (COVID−19) elicited by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS−CoV−2) is calling for novel targeted drugs. Since the viral entry into host cells depends on specific interactions between the receptor−binding domain (RBD) of the viral Spike protein and the membrane−bound monocarboxypeptidase angiotensin converting enzyme 2 (ACE2), the development of high affinity RBD binders to compete with human ACE2 represents a promising strategy for the design of therapeutics to prevent viral entry. Here, we report the discovery of such a binder and its improvement via a combination of computational and experimental approaches. The binder micasin, a known fungal defensin from the dermatophytic fungus Microsporum canis with antibacterial activity, can dock to the crevice formed by the receptor−binding motif (RBM) of RBD via an extensive shape complementarity interface (855.9 Å2 in area) with numerous hydrophobic and hydrogen−bonding interactions. Using microscale thermophoresis (MST) technique, we confirmed that micasin and its C−terminal γ−core derivative with multiple predicted interacting residues exhibited a low micromolar affinity to RBD. Expanding the interface area of micasin through a single point mutation to 970.5 Å2 accompanying an enhanced hydrogen bond network significantly improved its binding affinity by six−fold. Our work highlights the naturally occurring fungal defensins as an emerging resource that may be suitable for the development into antiviral agents for COVID−19.

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Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Cited by 49 publications

References 290 publications

Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs

Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs

Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields

A Fungal Defensin Targets the SARS−CoV−2 Spike Receptor−Binding Domain

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