Rational design yields molecular insights on leaf binding of the anchor peptide Macaque Histatin

Abstract

In times of a constantly growing world population and increasing demand for food, sustainable agriculture is crucial. To reduce the amount of applied nutrients, herbicides, and fungicides, the rainfastness of plant protection agents is of pivotal importance. 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 is 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. While 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 leaf 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 MTP assay that mimicks these complex processes and allows 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.

Global plastic upcycling during and after the COVID-19 pandemic: The status and perspective

“…Industry-scale biodegradation was limited by the time-consuming natural processing, and as a result, enzyme discovery, protein engineering, kinetics, and computational studies provided potential solutions [129] , [130] , [131] , [132] , [133] , [134] , [135] , [136] . However, industrial application of biodegradating plastics using biocatalysts like carboxyl ester hydrolases, including lipases, esterases, cutinases, and PETases, have not been achieved yet due to a number of reasons (e.g., instability and activity reduction in even mild conditions) [133] .…”

“…Son et al also reported a ThermoPETase variant (S121E/D186H/R280A) with remarkably enhanced thermal stability with PET degradation ability [133] . Luckily, protein engineering is not limited to altering primary sequences but offers the opportunity to design complex enzyme structures through the fusion of extra functional domains or carbohydrate-binding modules [132] . Substrate accessibility is an essential step for carboxyl ester hydrolases working on the smooth and unnotched plastic surface.…”

“…Substrate accessibility is an essential step for carboxyl ester hydrolases working on the smooth and unnotched plastic surface. Dittrich et al found anchor peptides provide an unprecedented opportunity for bio-interface functionalization with the ability to irreversibly adsorb proteins to surfaces [132] , indicating the design of fusion depolymerases with adhesion-promoting anchor peptides is an efficient method to enhance depolymerases efficiency and binding efficiency on polymer surfaces [137] . Besides, Ribitsch et al improved the enzymatic binding affinity for hydrophobic PET surfaces by adding the hydrophobins.…”