Large-Scale Plasma Peptidomic Profiling Reveals a Novel, Nontoxic, Crassostrea hongkongensis-Derived Antimicrobial Peptide against Foodborne Pathogens

Mao, Fan; Bao, Yongbo; Wong, Nai-Kei; Huang, Minwei; Liu, Kunna; Zhang, Xiangyu; Yang, Zhuo; Yi, Wenjie; Shu, Xiao Ou; Xiang, Zhiming; Zhou, Yu; Zhang, Yang

doi:10.3390/md19080420

Cited by 14 publications

(7 citation statements)

References 42 publications

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“…The hydrophobicity of ABPs is another distinguishing feature, and the lipid bilayer that makes up the microbial membrane is hydrophobic in nature [ 55 ]. The hydrophobic residues also promote the interaction of the peptide with phospholipid membranes, increasing the bactericidal effect of the peptide [ 56 ] Ser-Thr-Ile-Arg and Ala-Gly-Gly-Val-Pro-Arg due to the presence of hydrophobic amino acid residues Ile, Ala, and Pro, whose presence contributes to the efficient inhibitory activity of this peptide [ 57 ]. This may also explain the stronger bacterial inhibition of the peptide Ala-Gly-Gly-Val-Pro-Arg than Ser-Thr-Ile-Arg.…”

Section: Discussionmentioning

confidence: 99%

Antibacterial Effect of Sesame Protein-Derived Peptides against Escherichia coli and Staphylococcus aureus: In Silico and In Vitro Analysis

Zhu,

Pan,

Wang

et al. 2024

Nutrients

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This study aimed to screen out antibacterial peptides derived from sesame (Sesamum indicum L.) through in silico and in vitro methods. In silico proteolysis of sesame proteins with pepsin, trypsin, and chymotrypsin was performed with the online server BIOPEP-UWM. The CAMPR3 online server was used to predict the antimicrobial effect of peptides. The ToxinPred, PepCalc, and AllergenFP tools were utilized to forecast the physicochemical properties, toxicity, and allergen of the peptides. Molecular docking analysis showed that six cationic antimicrobial peptides could directly interact with the key sites of dihydropteroate synthase, whereas Ala-Gly-Gly-Val-Pro-Arg and Ser-Thr-Ile-Arg exhibited the strongest binding affinity. In vitro antibacterial experiment showed the minimum inhibitory concentration (MIC) of Ser-Thr-Ile-Arg against Escherichia coli and Staphylococcus aureus was 1024 and 512 µg/mL, respectively. Meanwhile, MIC of Ala-Gly-Gly-Val-Pro-Arg against both bacterial species was 512 µg/mL. Our results suggest that peptides from sesame possess the ability to potentially hinder bacterial activity.

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Section: Discussionmentioning

confidence: 99%

Antibacterial Effect of Sesame Protein-Derived Peptides against Escherichia coli and Staphylococcus aureus: In Silico and In Vitro Analysis

Zhu,

Pan,

Wang

et al. 2024

Nutrients

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“…Endogenous peptides are considered multifunctional and have been found to be involved in numerous biological processes. Peptidomics is an emerging branch of proteomics that targets endogenously produced protein fragments [ 43 , 44 ]. Differential and quantitative peptidome analysis of different samples exhibits a differential peptidomic profile.…”

Section: Discussionmentioning

confidence: 99%

Tat-hspb1 Suppresses Clear Cell Renal Cell Carcinoma (ccRCC) Growth via Lysosomal Membrane Permeabilization

Zhang

Jin

Liu

2022

Cancers

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Clear cell renal cell carcinoma (ccRCC) is the most prevalent kidney cancer, of which the incidence is increasing worldwide with a high mortality rate. Bioactive peptides are considered a significant class of natural medicines. We applied mass spectrometry-based peptidomic analysis to explore the peptide profile of human renal clear cell carcinoma and adjacent normal tissues. A total of 18,031 peptides were identified, of which 105 unique peptides were differentially expressed (44 were up-regulated and 61 were down-regulated in ccRCC tissues). Through bioinformatic analysis, we finally selected one peptide derived from the HSPB1 protein (amino acids 12–35 of the N-terminal region of HSPB1). Next, we fused this peptide to the HIV-Tat, generated a novel peptide named Tat-hspb1, and found that Tat-hspb1 inhibited ccRCC cells’ viability while being less cytotoxic to normal epithelial cells. Furthermore, Tat-hspb1 induced apoptosis and inhibited the proliferation and migration of ccRCC cells. Furthermore, we demonstrated that Tat-hspb1 was predominantly localized in lysosomes after entering the ccRCC cell and induced lysosomal membrane permeabilization (LMP) and the release of cathepsin D from lysosomes. Taken together, Tat-hspb1 has the potential to serve as a new anticancer drug candidate.

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“…To assess the membrane permeability induced by Np HM4, the high-affinity nucleic acid stain SYTOX ® Green (S7020, Thermo Fisher, Waltham, MA, USA) was used, as it easily penetrates cells with compromised plasma membranes [ 60 ]. Briefly, V. alginolyticus was cultured to the logarithmic growth phase and harvested via centrifugation at 2000× g for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Functional Characterization, Antimicrobial Effects, and Potential Antibacterial Mechanisms of NpHM4, a Derived Peptide of Nautilus pompilius Hemocyanin

et al. 2022

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Hemocyanins present in the hemolymph of invertebrates are multifunctional proteins that are responsible for oxygen transport and play crucial roles in the immune system. They have also been identified as a source of antimicrobial peptides during infection in mollusks. Hemocyanin has also been identified in the cephalopod ancestor Nautilus, but antimicrobial peptides derived from the hemocyanin of Nautilus pompilius have not been reported. Here, the bactericidal activity of six predicted peptides from N. pompilius hemocyanin and seven mutant peptides was analyzed. Among those peptides, a mutant peptide with 15 amino acids (1RVFAGFLRHGIKRSR15), NpHM4, showed relatively high antibacterial activity. NpHM4 was determined to have typical antimicrobial peptide characteristics, including a positive charge (+ 5.25) and a high hydrophobic residue ratio (40%), and it was predicted to form an alpha-helical structure. In addition, NpHM4 exhibited significant antibacterial activity against Gram-negative bacteria (MBC = 30 μM for Vibrio alginolyticus), with no cytotoxicity to mammalian cells even at a high concentration of 180 µM. Upon contact with V. alginolyticus cells, we confirmed that the bactericidal activity of NpHM4 was coupled with membrane permeabilization, which was further confirmed via ultrastructural images using a scanning electron microscope. Therefore, our study provides a rationalization for the development and optimization of antimicrobial peptide from the cephalopod ancestor Nautilus, paving the way for future novel AMP development with broad applications.

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Large-Scale Plasma Peptidomic Profiling Reveals a Novel, Nontoxic, Crassostrea hongkongensis-Derived Antimicrobial Peptide against Foodborne Pathogens

Cited by 14 publications

References 42 publications

Antibacterial Effect of Sesame Protein-Derived Peptides against Escherichia coli and Staphylococcus aureus: In Silico and In Vitro Analysis

Antibacterial Effect of Sesame Protein-Derived Peptides against Escherichia coli and Staphylococcus aureus: In Silico and In Vitro Analysis

Tat-hspb1 Suppresses Clear Cell Renal Cell Carcinoma (ccRCC) Growth via Lysosomal Membrane Permeabilization

Functional Characterization, Antimicrobial Effects, and Potential Antibacterial Mechanisms of NpHM4, a Derived Peptide of Nautilus pompilius Hemocyanin

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