Dataset Information

Leveraging Arylboronic Acid - Cellulose Binding as a Versatile and Scalable Approach to Hydrophobic Patterning.

ABSTRACT: Paper-based analytical devices, or μPADs, have proven to be valuable bioanalytical tools for a broad range of applications. New methods for μPAD fabrication are needed, however, to facilitate their mass production at a competitive cost. To address this need, we report the use of a boronic acid-containing siloxane polymer (BorSilOx) for patterning hydrophobic barriers for μPADs. This material functions by covalently binding to hydroxyl groups in the paper substrate. It is compatible with inkjet printing or roll-to-roll (stamping) processes, as demonstrated here using three different deposition methods. BorSilOx is able to render a broad range of cellulosic materials (from paper towels to wood) hydrophobic, with contact angle measurements demonstrating superhydrophobicity in many cases. We further demonstrate the utility of the polymer in μPADs via assays for pH and glucose.

SUBMITTER: Beard JW

PROVIDER: S-EPMC9355117 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Leveraging Arylboronic Acid - Cellulose Binding as a Versatile and Scalable Approach to Hydrophobic Patterning.

Beard Jeffrey W JW Murty Shannon S Caulkins Christina C Strenk Amanda R AR Luta Ethan P EP Hunt Samuel L SL Yates Matthew Z MZ Miller Benjamin L BL

Advanced materials technologies 20211216 7

Paper-based analytical devices, or μPADs, have proven to be valuable bioanalytical tools for a broad range of applications. New methods for μPAD fabrication are needed, however, to facilitate their mass production at a competitive cost. To address this need, we report the use of a boronic acid-containing siloxane polymer (BorSilOx) for patterning hydrophobic barriers for μPADs. This material functions by covalently binding to hydroxyl groups in the paper substrate. It is compatible with inkjet p ...[more]

PMID: 35935145

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Project description:BackgroundThe major birch pollen allergen, Bet v 1, is a member of the ubiquitous PR-10 family of plant pathogenesis-related proteins. In recent years, a number of diverse plant proteins with low sequence similarity to Bet v 1 was identified. In addition, determination of the Bet v 1 structure revealed the existence of a large superfamily of structurally related proteins. In this study, we aimed to identify and classify all Bet v 1-related structures from the Protein Data Bank and all Bet v 1-related sequences from the Uniprot database.ResultsStructural comparisons of representative members of already known protein families structurally related to Bet v 1 with all entries of the Protein Data Bank yielded 47 structures with non-identical sequences. They were classified into eleven families, five of which were newly identified and not included in the Structural Classification of Proteins database release 1.71. The taxonomic distribution of these families extracted from the Pfam protein family database showed that members of the polyketide cyclase family and the activator of Hsp90 ATPase homologue 1 family were distributed among all three superkingdoms, while members of some bacterial families were confined to a small number of species. Comparison of ligand binding activities of Bet v 1-like superfamily members revealed that their functions were related to binding and metabolism of large, hydrophobic compounds such as lipids, hormones, and antibiotics. Phylogenetic relationships within the Bet v 1 family, defined as the group of proteins with significant sequence similarity to Bet v 1, were determined by aligning 264 Bet v 1-related sequences. A distance-based phylogenetic tree yielded a classification into 11 subfamilies, nine exclusively containing plant sequences and two subfamilies of bacterial proteins. Plant sequences included the pathogenesis-related proteins 10, the major latex proteins/ripening-related proteins subfamily, and polyketide cyclase-like sequences.ConclusionThe ubiquitous distribution of Bet v 1-related proteins among all superkingdoms suggests that a Bet v 1-like protein was already present in the last universal common ancestor. During evolution, this protein diversified into numerous families with low sequence similarity but with a common fold that succeeded as a versatile scaffold for binding of bulky ligands.

Dataset Information

Leveraging Arylboronic Acid - Cellulose Binding as a Versatile and Scalable Approach to Hydrophobic Patterning.

Publications

Leveraging Arylboronic Acid - Cellulose Binding as a Versatile and Scalable Approach to Hydrophobic Patterning.

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