ArticleEuropean biophysics journal : EBJ2007
Hydrophobic interactions are the driving force for the binding of peptide mimotopes and Staphylococcal protein A to recombinant human IgG1.
Article in European biophysics journal : EBJ, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Revealing the Dualistic Toxicity of 1,4-Naphthoquinone in Earthworms: Cytotoxic Damage in Coelomocytes and Spectroscopic Insights Into Catalase Activation.Luminescence : the journal of biological and chemical luminescence · 2026Article
- Investigating the Nature of PRM:SH3 Interactions Using Artificial Intelligence and Molecular Dynamics.Journal of chemical information and modeling · 2025Article
- Green Tea Pressurized Hot Water Extract in Atherosclerosis: A Multi-Approach Study on Cellular, Animal, and Molecular Mechanisms.Antioxidants (Basel, Switzerland) · 2025Article
- Design of inhibitor peptide sequences based on the interfacial knowledge of the protein G-IgG crystallographic complex and their binding studies with IgG.European biophysics journal : EBJ · 2024Article
- Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases.PloS one · 2017Article
- Cysteine-terminated B-domain of Staphylococcus aureus protein A as a scaffold for targeting GABA(A) receptors.Analytical biochemistry · 2013Article
- Insights into protein-polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry.European biophysics journal : EBJ · 2009Article
- Optical tweezers to study single protein A/immunoglobulin G interactions at varying conditions.European biophysics journal : EBJ · 2008Article
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Authors and funding
4 authors.
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Abstract
We studied the interaction of several nona-peptide mimotopes of different sequence and Staphylococcal protein A (SpA) with a recombinant human IgG1 antibody using isothermal titration calorimetry (ITC). The amino acid primary structure of the peptides was varied in order to identify the specific antibody-peptide binding sites. Additionally, the influence of temperature and salt concentration was investigated. An attempt was made to elucidate the structural changes upon complex formation using the determined thermodynamic parameters. The amino acid composition of the mimotopes determined their binding affinity. The binding constant K (a) of the mimotopes was in the range 1 x 10(4) to 1 x 10(6) M(-1). The binding constant of SpA was on the average about three orders of magnitude higher than that of the peptides. The binding constant of the peptides and of SpA decreased with temperature and the binding process was connected with negative changes in enthalpy, entropy, and heat capacity. The binding of the mimotopes to the Fab part of the IgG1 antibody and binding of SpA to the Fc part of the IgG1 antibody were mainly driven by hydrophobic effects and associated with a relatively large change in water-accessible surface area. Determinants for a strong/reduced antibody-peptide binding were identified.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.