ArticleBiophysical journal2022
Modulating binding affinity, specificity, and configurations by multivalent interactions.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
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- Effects of gestational perfluorohexanesulfonic acid exposure at human realistic dose on social communication deficit in mouse offspring.EBioMedicine · 2026Article
- DNA co-recognition and pH dependent regulation mechanism of zinc finger domain and C-terminal basic region of CreA in Aspergillus.Archives of microbiology · 2026Article
- STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.Molecular neurodegeneration advances · 2026Article
- Update on Structure and Function of SH2 Domains: Mechanisms and Emerging Targeting Strategies.International journal of molecular sciences · 2025Review
- Radioiodinated Bicyclic RGD Peptide Derivatives for Enhanced Tumor Accumulation.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Fluctuations in Medium Viscosity May Affect the Stability of the CAG Tract in theBiomedicines · 2024Article
- Sugar-Coated: Can Multivalent Glycoconjugates Improve upon Nature's Design?Journal of the American Chemical Society · 2024Review
- Multivalent Protein-Nucleic Acid Interactions Probed by Composition-Gradient Multiangle Light Scattering.ACS omega · 2024Article
- A Multivalent DNA Nanoparticle/Peptide Hybrid Molecular Modality for the Modulation of Protein-Protein Interactions in the Tumor Microenvironment.Advanced nanobiomed research · 2024Article
- Identifying Residues for Substrate Recognition in Human GPAT4 by Molecular Dynamics Simulations.International journal of molecular sciences · 2024Article
- Exploring TRF2-Dependent DNA Distortion Through Single-DNA Manipulation Studies.Communications biology · 2024Article
- Tryptophan mutations in G3BP1 tune the stability of a cellular signaling hub by weakening transient interactions with Caprin1 and USP10.The Journal of biological chemistry · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological functions of proteins rely on their specific interactions with binding partners. Many proteins contain multiple domains, which can bind to their targets that often have more than one binding site, resulting in multivalent interactions. While it has been shown that multivalent interactions play a crucial role in modulating binding affinity and specificity, other potential effects of multivalent interactions are less explored. Here, we developed a broadly applicable transfer-matrix formalism and used it to investigate the binding of two-domain ligands to targets with multiple binding sites. We show that 1) ligands with two specific binding domains can drastically boost both the binding affinity and specificity and downshift the working concentration range, compared with single-domain ligands, 2) the presence of a positive domain-domain cooperativity or containing a nonspecific binding domain can downshift the working concentration range of ligands by increasing the binding affinity without compromising the binding specificity, and 3) the configuration of the bound ligands has a strong concentration dependence, providing important insights into the physical origin of phase-separation processes taking place in living cells. In line with previous studies, our results suggest that multivalent interactions are utilized by cells for highly efficient regulation of target binding involved in a diverse range of cellular processes such as signal transduction, gene transcription, and antibody-antigen recognition.
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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.