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Rational Design Yields Molecular Insights on Leaf-Binding of Anchor Peptides
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Researchers developed the first atomistic three-layered model of apple leaf surfaces to compute free energy profiles of anchor peptide adhesion and desorption, validating predictions with a novel fluorescence-based microtiter plate assay. They found that aromatic and positively charged residues in anchor peptides drive adhesion to the complex polysaccharide-coated leaf surface, offering a biodegradable alternative to polymeric adjuvants that would otherwise contribute to microplastic pollution.
In times of a constantly growing world population and increasing demand for food, sustainable agriculture is crucial. The rainfastness of plant protection agents is of pivotal importance to reduce the amount of applied nutrients, herbicides, and fungicides. As a result of protective agent wash-off, plant protection is lost, and soils and groundwater are severely polluted. To date, rainfastness of plant protection products has been achieved by adding polymeric adjuvants to the agrochemicals. However, polymeric adjuvants will be regarded as microplastics in the future, and environmentally friendly alternatives are needed. Anchor peptides (APs) are promising biobased and biodegradable adhesion promoters. Although the adhesion of anchor peptides to artificial surfaces, such as polymers, has already been investigated in theory and experimentally, exploiting the adhesion to biological surfaces remains challenging. The complex nature and composition of biological surfaces such as plant leaves and fruit surfaces complicate the generation of accurate models. Here, we present the first detailed three-layered atomistic model of the surface of apple leaves and use it to compute free energy profiles of the adhesion and desorption of APs to and from that surface. Our model is validated by a novel fluorescence-based microtiter plate (MTP) assay that mimics these complex processes and allows for quantifying them. For the AP Macaque Histatin, we demonstrate that aromatic and positively charged amino acids are essential for binding to the waxy apple leaf surface. The established protocols should generally be applicable for tailoring the binding properties of APs to biological interfaces.
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This study used rational peptide design to engineer an anchor peptide from Macaque Histatin-1 that binds to plant leaves to improve the rainfastness of agrochemicals. The approach aims to replace polymeric adjuvants, which would be classified as microplastics, with biodegradable peptide-based alternatives.
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Researchers developed a computational physics-based approach to design peptides that bind to plastic surfaces, with the goal of functionalizing surfaces or assisting in interfacial self-assembly. This in silico method offers an alternative to traditional peptide library screening and provides physical insight into the basis of peptide-plastic affinity.
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Researchers used molecular modeling and experiments to investigate how peptides form eco-corona layers on polyethylene microplastic surfaces, finding that peptide adsorption is governed by amino acid hydrophobicity and surface chemistry. The study provides molecular-level insight into how plastics integrate into biological environments by binding proteins and peptides.
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This review covers material-binding peptides, which are short protein fragments that can attach to specific materials including plastics. These peptides have promising applications in detecting and quantifying microplastics in the environment, as well as potentially accelerating plastic degradation. The technology draws on advances in protein engineering and computational design.
Peptide Corona Formation on Polyethylene Surfaces: A Combined Computational and Experimental Study
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Researchers used a combination of molecular dynamics simulations and experiments to study how peptides from food and biological systems form coronas on polyethylene microplastic surfaces. They found that peptide adsorption is governed by amino acid hydrophobicity and surface potential, altering both the plastic particle behavior and the bound peptides' biological activity.
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