Stability and antiviral activity of SP40 peptide in human serum

Zarif, Faisal; Anasir, Mohd Ishtiaq; Koh, Jia Xuen; Chew, Miaw-Fang; Poh, Chit Laa

doi:10.1016/j.virusres.2021.198456

Cited by 7 publications

(4 citation statements)

References 44 publications

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“…Supplementary Fig [44][45][46][47][48][49][50][51][52][53] show serum stability studies; these were monitored by analytical HPLC and LC-MS to enable detection of degradation products. BAMM containing mimics (red) prevented degradation from the N-termini, and stability enhancements relative to controls were greatest for shorter systems (1-3) where BAMM can block peptidases most effectively.…”

Section: Bamm-containing Analogs Of Natural Interface Helicesmentioning

confidence: 99%

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Bioinformatics leading to conveniently accessible, helix enforcing, bicyclic ASX motif mimics (BAMMs)

Mi,

Nguyen,

Gao

et al. 2024

Nat Commun

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Helix mimicry provides probes to perturb protein-protein interactions (PPIs). Helical conformations can be stabilized by joining side chains of non-terminal residues (stapling) or via capping fragments. Nature exclusively uses capping, but synthetic helical mimics are heavily biased towards stapling. This study comprises: (i) creation of a searchable database of unique helical N-caps (ASX motifs, a protein structural motif with two intramolecular hydrogen-bonds between aspartic acid/asparagine and following residues); (ii) testing trends observed in this database using linear peptides comprising only canonical L-amino acids; and, (iii) novel synthetic N-caps for helical interface mimicry. Here we show many natural ASX motifs comprise hydrophobic triangles, validate their effect in linear peptides, and further develop a biomimetic of them, Bicyclic ASX Motif Mimics (BAMMs). BAMMs are powerful helix inducing motifs. They are synthetically accessible, and potentially useful to a broad section of the community studying disruption of PPIs using secondary structure mimics.

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Section: Bamm-containing Analogs Of Natural Interface Helicesmentioning

confidence: 99%

“…In vitro peptide stability in human serum 50 Male human serum (H-4522) was obtained from Sigma Aldrich (Missouri, USA). The tested peptide was mixed to make a final peptide concentration of 150 μM in 25% human serum diluted in RPMI medium.…”

Section: Analysis: Bicyclic Peptides With L-cys and D-cysmentioning

confidence: 99%

Bioinformatics leading to conveniently accessible, helix enforcing, bicyclic ASX motif mimics (BAMMs)

Mi,

Nguyen,

Gao

et al. 2024

Nat Commun

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“…A zwitterionic peptide is a type of short-chain amino acid monomer connected by amide bonds, deemed as an ideal antifouling material. , Owing to the structural features, biocompatibility, and bioactivity, peptides have attracted widespread attention, especially in biomedical applications. , However, peptide embraces the characteristics of inherent instability and is apt to be degraded by protease under physiological conditions, − which severely limits their clinical application. To get over this shortcoming, several tactics have been employed to gain enhanced stability of the peptides, including cyclization and introduction of unnatural amino acids into peptide segments .…”

mentioning

confidence: 99%

Robust Electrochemical Biosensors Based on Antifouling Peptide Nanoparticles for Protein Quantification in Complex Biofluids

Song,

Li,

et al. 2024

ACS Sens.

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Peptides with distinct physiochemical properties and biocompatibility hold significant promise across diverse domains including antifouling biosensors. However, the stability of natural antifouling peptides in physiological conditions poses significant challenges to their viability for sustained practical applications. Herein, a unique antifouling peptide FFFGGGEKEKEKEK was designed and self-assembled to form peptide nanoparticles (PNPs), which possessed enhanced stability against enzymatic hydrolysis in biological fluids. The PNP-coated interfaces exhibited superior stability and antifouling properties in preventing adsorption of nonspecific materials, such as proteins and cells in biological samples. Moreover, a highly sensitive and ultralow fouling electrochemical biosensor was developed through the immobilization of the PNPs and specific aptamers onto the polyaniline nanowire-modified electrode, achieving the biomarker carcinoembryonic antigen detection in complex biofluids with reliable accuracy. This research not only addresses the challenge of the poor proteolytic resistance observed in natural peptides but also introduces a universal strategy for constructing ultralow fouling sensing devices.

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“…Despite peptides’ favorable antifouling property, the activity of proteolytic enzymes limits peptide antifouling-based electrochemical sensor performance in complicated environments. − Therefore, the regulation measures extremely need to improve their tolerance of antifouling coating with continuous long-term monitoring in vitro. Until now, significant strategies to protect biologically active peptides from enzymatic decomposition have been adopted to enhance the biological stability of various peptides, such as the conjugation of cyclization and the incorporation of unnaturally prepared amino acids, , such as d -amino acid, 2-aminoisobutric acid, and β-amino acid .…”

mentioning

confidence: 99%

d-Amino Acid-Based Antifouling Peptides for the Construction of Electrochemical Biosensors Capable of Assaying Proteins in Serum with Enhanced Stability

et al. 2022

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The susceptibility of peptides to proteolytic degradation in human serum significantly hindered the potential application of peptide-based antifouling biosensors for long-term assaying of clinical samples. Herein, a robust antifouling biosensor with enhanced stability was constructed based on peptides composed of D-amino acids (D-peptide) with prominent proteolytic resistance. The electrode was electropolymerized with poly(3,4-ehtylenedioxythiophene) and electrodeposited with Au nanoparticles (AuNPs), and the D-peptide was then immobilized onto the AuNPs, and a typical antibody specific for immunoglobulin M (IgM) was immobilized. Because of the effect of D-amino acids, the D-peptide-modified electrode surface showed prominent antifouling capability and high tolerance to enzymatic hydrolysis. Moreover, the D-peptide-modified electrode exhibited much stronger long-term stability, as well as antifouling ability in human serum than the electrode modified with normal peptides. The electrochemical biosensor exhibited a sensitive response to IgM linearly within the range of 100 pg mL −1 to 1.0 μg mL −1 and a very low detection limit down to 37 pg mL −1 , and it was able to detect IgM in human serum with good accuracy. This work provided a new strategy to develop robust peptide-based biosensors to resist the proteolytic degradation for practical application in complex clinical samples.

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Stability and antiviral activity of SP40 peptide in human serum

Cited by 7 publications

References 44 publications

Bioinformatics leading to conveniently accessible, helix enforcing, bicyclic ASX motif mimics (BAMMs)

Bioinformatics leading to conveniently accessible, helix enforcing, bicyclic ASX motif mimics (BAMMs)

Robust Electrochemical Biosensors Based on Antifouling Peptide Nanoparticles for Protein Quantification in Complex Biofluids

d-Amino Acid-Based Antifouling Peptides for the Construction of Electrochemical Biosensors Capable of Assaying Proteins in Serum with Enhanced Stability

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