Anchor Peptide-Mediated Surface Immobilization of a Grubbs-Hoveyda-Type Catalyst for Ring-Opening Metathesis Polymerization

Grimm, Alexander R.; Sauer, Daniel F.; Garakani, Tayebeh Mirzaei; Rübsam, Kristin; Polen, Tino; Davari, Mehdi D.; Jakob, Felix; Schiffels, Johannes; Okuda, Jun; Schwaneberg, Ulrich

doi:10.1021/acs.bioconjchem.8b00874

Cited by 17 publications

(15 citation statements)

References 32 publications

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“…Schwanberg et al coupled the thiolated polypeptide LCI using a Grubbs-Hoveyda (GH) type catalyst 89,90 and mutated the coupled polypeptide LCI to construct a silica material binding element GH1@LCI_F16C. 59 In order to apply the versatility of materials and improve the properties of the material surface, they combined this modified peptide with solid SiO 2 and polypropylene (PP) to make the material both catalytic and hydrophilic. The results showed that the contact angle of SiO 2 after fixation with LCI_F16C was reduced from 59°to 40°.…”

Section: Applications Of Peptides Combined With Inorganic Materialsmentioning

confidence: 99%

Applications of Material-Binding Peptides: A Review

Ruan

Sohail

Zhao

et al. 2022

ACS Biomater. Sci. Eng.

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Material-binding peptides (MBPs) are functionalized adhesive materials consisting of a few to several dozen amino acids. This affinity between MBPs and materials is regulated by multiple interactions, including hydrogen bonding, electrostatic, hydrophobic interactions, and π–π stacking. They show selective binding and high affinity to a diverse range of inorganic and organic materials, such as silicon-based materials, metals, metal compounds, carbon materials, and polymers. They are used to improve the biocompatibility of materials, increase the efficiency of material synthesis, and guide the controlled synthesis of nanomaterials. In addition, these can be used for precise targeting of proteins by conjugating to target biomolecules. In this review, we summarize the main designs and applications of MBPs in recent years. The discussions focus on more efficient and functional peptides, including evolution and overall design of MBPs. We have also highlighted the recent applications of MBPs, such as functionalization of material surfaces, synthesis of nanomaterials, drug delivery, cancer therapy, and plastic degradation. Besides, we also discussed the development trend of MBPs. This interpretation will accelerate future investigations to bottleneck the drawbacks of available MBPs, promoting their commercial applications.

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Section: Applications Of Peptides Combined With Inorganic Materialsmentioning

confidence: 99%

Applications of Material-Binding Peptides: A Review

Ruan

Sohail

Zhao

et al. 2022

ACS Biomater. Sci. Eng.

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“…Anchor peptides (APs) are short amphiphilic peptides with sizes ranging from 20 to 100 amino acids that bind from aqueous solutions to natural , and synthetic surfaces − including metals. , Tailor-made APs are thus applicable in many fields, including biotechnology, catalysis, nanoparticles, medicine, and agriculture …”

Section: Introductionmentioning

confidence: 99%

Rational Design Yields Molecular Insights on Leaf-Binding of Anchor Peptides

Dittrich

Brethauer

Goncharenko

et al. 2022

ACS Appl. Mater. Interfaces

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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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“…Anchor peptides (APs) are short amphiphilic peptides with sizes ranging from 20 to 100 amino acids that bind from aqueous solutions to natural [9][10] and synthetic surfaces [11][12][13][14] including metals [15][16] . Tailor-made APs are thus applicable in many fields, including biotechnology, 17 catalysis, 18 nanoparticles, 19 medicine, 20 and agriculture 9 .…”

Section: Introductionmentioning

confidence: 99%

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

Dittrich

Brethauer

Goncharenko

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Anchor Peptide-Mediated Surface Immobilization of a Grubbs-Hoveyda-Type Catalyst for Ring-Opening Metathesis Polymerization

Cited by 17 publications

References 32 publications

Applications of Material-Binding Peptides: A Review

Applications of Material-Binding Peptides: A Review

Rational Design Yields Molecular Insights on Leaf-Binding of Anchor Peptides

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

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