ArticleBiopolymers2018
The polypeptide biophysics of proline/alanine-rich sequences (PAS): Recombinant biopolymers with PEG-like properties.
Article in Biopolymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 64 citations in OpenAlex.
- CELLISA - a cell-cell binding assay for evaluation of nanovesicle targeting proteins.bioRxiv : the preprint server for biology · 2026Article
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Biosynthesized uricase with dual-terminus zwitterionic EKylation for prolonged elimination half-life and reduced immunogenicity.Journal of biological engineering · 2026Article
- Peptide and Protein Tags for the Half-Life Extension of Therapeutic Agents: A Review Article.The protein journal · 2026Review
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Structural Insights into the Protein Mannosyltransferase from Mycobacterium tuberculosis reveal a WW-Domain-Like Protein Motif in Bacteria.Communications biology · 2025Article
- Long-Acting Human PASylated Leptin Reaches the Murine Central Nervous System and Offers Potential for Optimized Replacement Therapy.Molecular pharmaceutics · 2025Article
- A versatile platform based on matrix metalloproteinase-sensitive peptides for novel diagnostic and therapeutic strategies in arthritis.Bioactive materials · 2025Review
- Enzyme-substrate co-display on yeast empowers engineering of tobacco etch virus protease activity.Protein engineering, design & selection : PEDS · 2025Article
- Determination ofRoyal Society open science · 2024Article
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- PASylated Urate Oxidase Enzyme: Enhancing Biocatalytic Activity, Physicochemical Properties, and Plasma Half-Life.ACS omega · 2022Article
- Efficient secretory production of proline/alanine/serine (PAS) biopolymers in Corynebacterium glutamicum yielding a monodisperse biological alternative to polyethylene glycol (PEG).Microbial cell factories · 2022Article
- Motif-based zwitterionic peptides impact their structure and immunogenicity.Chemical science · 2022Article
- Mapping the Morphological Landscape of Oligomeric Di-block Peptide-Polymer Amphiphiles.Angewandte Chemie (International ed. in English) · 2022Article
- Emerging Approaches to Functionalizing Cell Membrane-Coated Nanoparticles.Biochemistry · 2021Review
- Extended yeast surface display linkers enhance the enrichment of ligands in direct mammalian cell selections.Protein engineering, design & selection : PEDS · 2021Article
- PASylated Thymosin α1: A Long-Acting Immunostimulatory Peptide for Applications in Oncology and Virology.International journal of molecular sciences · 2020Article
- Proline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- PASylation of IL-1 receptor antagonist (IL-1Ra) retains IL-1 blockade and extends its duration in mouse urate crystal-induced peritonitis.The Journal of biological chemistry · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PAS polypeptides comprise long repetitive sequences of the small L-amino acids proline, alanine and/or serine that were developed to expand the hydrodynamic volume of conjugated pharmaceuticals and prolong their plasma half-life by retarding kidney filtration. Here, we have characterized the polymer properties both of the free polypeptides and in fusion with the biopharmaceutical IL-1Ra. Data from size exclusion chromatography, dynamic light scattering, circular dichroism spectroscopy and quantification of hydrodynamic and polar properties demonstrate that the biosynthetic PAS polypeptides exhibit random coil behavior in aqueous solution astonishingly similar to the chemical polymer poly-ethylene glycol (PEG). The solvent-exposed PAS peptide groups, in the absence of secondary structure, account for strong hydrophilicity, with negligible contribution by the Ser side chains. Notably, PAS polypeptides exceed PEG of comparable molecular mass in hydrophilicity and hydrodynamic volume while exhibiting lower viscosity. Their uniform monodisperse composition as genetically encoded polymers and their biological nature, offering biodegradability, render PAS polypeptides a promising PEG mimetic for biopharmaceutical applications.
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