Determining the Binding Kinetics of Peptide Macrocycles Using Bio-Layer Interferometry (BLI)

Rhea, Katherine

doi:10.1007/978-1-0716-1689-5_19

Cited by 5 publications

(3 citation statements)

References 7 publications

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“…Biolayer interferometry (BLI) enables the detection of molecular interactions in real time without the hassle and interference of labeling. 35 The affinity constant (K d ) obtained in the BLI analysis is a key indicator to evaluate the binding and dissociation of umami peptides and T1R1-VFT. 36 The binding−dissociation curves between umami peptides with T1R1-VFT at different concentrations are shown in Figure S3.…”

Section: Kinetic Analysis 331 Based On Biolayermentioning

confidence: 99%

Novel Umami Peptides from Mushroom (Agaricus bisporus) and Their Umami Enhancing Effect via Virtual Screening and Molecular Simulation

Xu,

Chen,

Cui

et al. 2024

J. Agric. Food Chem.

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This study aimed to identify novel umami peptides in Agaricus bisporus and investigate their umami enhancing effect. We virtually screened 155 potential umami peptides from the ultrasound-assisted A. bisporus hydrolysate according to Q values, iUmami-SCM, Umami_YYDS, and Tastepeptides_DM models, and molecular docking. Five peptides (AGKNTNGSQF, DEAVARGATF, REESDFQSSF, SEETTTGVHH, and WNNDAFQSSTN) were synthesized for sensory evaluation and kinetic analysis. The result showed that the umami thresholds of the five peptides were in the range of 0.21−0.40 mmol/L. Notably, REESDFQSSF, SEETTTGVHH, and WNNDAFQSSTN had low dissociation constant (K D ) values and high affinity for the T1R1-VFT receptor. The enhancing effect of the three peptides with MSG or IMP was investigated by sensory evaluation, kinetic analysis, and molecular dynamics simulations. In stable complexes, ARG_277 in T1R1 played a major role in umami peptide binding to T1R1-VFT. These results provide a theoretical basis for future screening of umami peptides and improving the umami taste of food containing mushrooms.

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Section: Kinetic Analysis 331 Based On Biolayermentioning

confidence: 99%

Novel Umami Peptides from Mushroom (Agaricus bisporus) and Their Umami Enhancing Effect via Virtual Screening and Molecular Simulation

Xu,

Chen,

Cui

et al. 2024

J. Agric. Food Chem.

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“…These homing peptides have previously been reported to have a high binding affinity for target sites in nanomolar concentrations 57 . To determine their binding affinity, a variety of techniques can be used, including surface-enhanced raman scattering (SERS) 58 , bio-layer interferometry (BLI) 59 , isothermal titration calorimetry (ITC), and drug affinity responsive target stability (DARTS) ( Fig. 2 ).…”

Section: Peptides In Pdcsmentioning

confidence: 99%

Peptide–drug conjugates (PDCs): a novel trend of research and development on targeted therapy, hype or hope?

Miao

et al. 2023

Acta Pharmaceutica Sinica B

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“…Similar to surface plasmon resonance, biolayer interferometry (BLI) provides fast, label-free, and real-time detection of antigen-antibody interactions and provides information about interaction affinity and kinetics [ 86 – 88 ]. Some examples of BLI assays include and label-free measurements of monoclonal antibody therapeutics (LOQs 2–10 µg/mL in serum) and detection of anti-COVID-19 antibodies [ 89 – 92 ].…”

Section: Main Textmentioning

confidence: 99%

Redefining serological diagnostics with immunoaffinity proteomics

Walter,

Eludin,

Drabovich

2023

Clin Proteom

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Serological diagnostics is generally defined as the detection of specific human immunoglobulins developed against viral, bacterial, or parasitic diseases. Serological tests facilitate the detection of past infections, evaluate immune status, and provide prognostic information. Serological assays were traditionally implemented as indirect immunoassays, and their design has not changed for decades. The advantages of straightforward setup and manufacturing, analytical sensitivity and specificity, affordability, and high-throughput measurements were accompanied by limitations such as semi-quantitative measurements, lack of universal reference standards, potential cross-reactivity, and challenges with multiplexing the complete panel of human immunoglobulin isotypes and subclasses. Redesign of conventional serological tests to include multiplex quantification of immunoglobulin isotypes and subclasses, utilize universal reference standards, and minimize cross-reactivity and non-specific binding will facilitate the development of assays with higher diagnostic specificity. Improved serological assays with higher diagnostic specificity will enable screenings of asymptomatic populations and may provide earlier detection of infectious diseases, autoimmune disorders, and cancer. In this review, we present the major clinical needs for serological diagnostics, overview conventional immunoassay detection techniques, present the emerging immunoassay detection technologies, and discuss in detail the advantages and limitations of mass spectrometry and immunoaffinity proteomics for serological diagnostics. Finally, we explore the design of novel immunoaffinity-proteomic assays to evaluate cell-mediated immunity and advance the sequencing of clinically relevant immunoglobulins.

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Determining the Binding Kinetics of Peptide Macrocycles Using Bio-Layer Interferometry (BLI)

Cited by 5 publications

References 7 publications

Novel Umami Peptides from Mushroom (Agaricus bisporus) and Their Umami Enhancing Effect via Virtual Screening and Molecular Simulation

Novel Umami Peptides from Mushroom (Agaricus bisporus) and Their Umami Enhancing Effect via Virtual Screening and Molecular Simulation

Peptide–drug conjugates (PDCs): a novel trend of research and development on targeted therapy, hype or hope?

Redefining serological diagnostics with immunoaffinity proteomics

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