ArticleBMC biotechnology2013
Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity.
Article in BMC biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Molecular Engineering of Recombinant Protein Hydrogels: Programmable Design and Biomedical Applications.Gels (Basel, Switzerland) · 2025Review
- Optimized cutaneous delivery of anti-wrinkle dipeptide KT via molecular modification: Preformulation, permeation, and the importance of conjugate chain length.BioImpacts : BI · 2025Article
- Collagen-targeted protein nanomicelles for the imaging of non-alcoholic steatohepatitis.Acta biomaterialia · 2024Article
- Peptide Amphiphiles as Biodegradable Adjuvants for Efficient Retroviral Gene Delivery.Advanced healthcare materials · 2024Article
- Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022Review
- Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.Frontiers in cellular and infection microbiology · 2021Review
- Impact of non-proteinogenic amino acids in the discovery and development of peptide therapeutics.Amino acids · 2020Review
- Current Trends of Bioactive Peptides-New Sources and Therapeutic Effect.Foods (Basel, Switzerland) · 2020Review
- Article
- Multivalent Peptide-Nanoparticle Conjugates for Influenza-Virus Inhibition.Angewandte Chemie (International ed. in English) · 2017Article
- Review
- Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1.Frontiers in microbiology · 2013Article
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA promising way in diagnostic and therapeutic applications is the development of peptide amphiphiles (PAs). Peptides with a palmitic acid alkylchain were designed and characterized to study the effect of the structure modifications on self-assembling capabilities and the multiple binding capacity to hemagglutinin (HA), the surface protein of influenza virus type A. The peptide amphiphiles consists of a hydrophilic headgroup with a biological functionality of the peptide sequence and a chemically conjugated hydrophobic tail. In solution they self-assemble easily to micelles with a hydrophobic core surrounded by a closely packed peptide-shell.
resultsIn this study the effect of a multiple peptide binding partner to the receptor binding site of HA could be determined with surface plasmon resonance measurements. The applied modification of the peptides causes signal amplification in relationship to the unmodified peptide wherein the high constant specificity persists. The molecular assembly of the peptides was characterized by the determination of critical micelle concentration (CMC) with concentration of 10⁻⁵ M and the colloidal size distribution.
conclusionThe modification of the physico-chemical parameters by producing peptide amphiphiles form monomeric structures which enhances the binding affinity and allows a better examination of the interaction with the virus surface protein hemagglutinin.
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