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Peptides and proteins self-assemble into β-sheet-rich fibrils, amyloid, which extends its structure by incorporating peptide/protein molecules from solution. At the elongation edge, the peptide/protein molecule binds to the edge of the amyloid β-sheet. Such processes are transient and elusive when observing molecular details by experimental methods. We used a model protein system, peptide self-assembly mimic (PSAM), which mimics an amyloid-like structure within a globular protein by capping both edges of single-layer β sheet (SLB) with certain domains. We constructed a PSAM variant that lacks the capping domain on the C-terminal side to observe the structure of the β-sheet edge of the peptide self-assembly. This variant, which we termed PSAM-edge, proved to be soluble with a monomeric form. Urea-induced unfolding experiments revealed that PSAM-edge displayed two-state cooperative unfolding, indicating the N-terminal capping domain and extended SLB folded as one unit. The crystal structure showed that SLB was almost completely structured except for a few terminal residues. A molecular dynamics simulation results revealed that the SLB structure was retained while the C-terminal four residues fluctuated, which was consistent with the crystal structure. Our findings indicate that SLB is stable even when one side of the β-sheet edge is exposed to a solvent. This stability may prevent the dissociation of the attached peptide from the peptide self-assembly. Because of the scarcity of SLB proteins with exposed β-sheet edges in nature, successful construction of the PSAM-edge expands our understanding of protein folding and design.
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http://dx.doi.org/10.1002/prot.26063 | DOI Listing |
Chem Sci
December 2024
Department of Chemistry, University of Warwick Coventry CV4 7AL UK
Self-assembling cyclic peptide nanotubes are fascinating supramolecular systems with promising potential for various applications, such as drug delivery, transmembrane ionic channels, and artificial light-harvesting systems. In this study, we present novel pH-responsive nanotubes based on asymmetric cyclic peptide-polymer conjugates. The pH response is introduced by a tertiary amine-based polymer, poly(dimethylamino ethyl methacrylate) (pDMAEMA) or poly(diethylamino ethyl methacrylate) (pDEAEMA) which is protonated at low pH.
View Article and Find Full Text PDFJ Biomed Mater Res A
January 2025
Department of Chemical & Biomolecular Engineering, University of Notre Dame, Notre Dame, USA.
Precise blood glucose control continues to be a critical challenge in the treatment and management of type 1 diabetes in order to mitigate both acute and chronic complications. This study investigates the development of a supramolecular peptide amphiphile (PA) material functionalized with phenylboronic acid (PBA) for glucose-responsive glucagon delivery. The PA-PBA system self-assembles into nanofibrillar hydrogels in the presence of physiological glucose levels, resulting in stable hydrogels capable of releasing glucagon under hypoglycemic conditions.
View Article and Find Full Text PDFBiopolymers
January 2025
Department of Biotechnology, National Institute of Technology Durgapur, Durgapur, West Bengal, India.
Dipeptides were constructed using hydrophobic amino acid residues following AMP prediction. After that Boc-modification was performed on the screened peptides and finally Boc-Phe-Trp-OMe and Boc-Trp-Trp-OMe were synthesized. Even though no inhibition zones were observed in agar well diffusion assays, minimum inhibitory concentration (MIC) analysis revealed anti-bacterial activity against both Gram-positive and Gram-negative bacteria, with MIC ranging from 230 to 400 μg/mL.
View Article and Find Full Text PDFSmall
December 2024
Chemical Biology Unit, Institute of Nano Science and Technology (INST), Sector 81, Mohali, Punjab, 140306, India.
Dynamic peptide networks represent an attractive structural space of supramolecular polymers in the realm of emergent complexity. Point mutations in the peptide sequence exert profound effects over the landscapes of self-assembly with an intricate interplay among the structure-function relationships. Herein, the pathway complexity of an arginine-rich peptide is studied, FmocVFFARR derived by the mutation of minimalist amyloid-inspired peptide amphiphile FmocVFFAKK, thereby focusing on its pathway-dependent self-assembly behavior.
View Article and Find Full Text PDFActa Biomater
December 2024
Division of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Missouri-Kansas City, 2464 Charlotte Street, Kansas City, MO 64108, USA. Electronic address:
Antibody-based checkpoint inhibitors have achieved great success in cancer immunotherapy, but their uncontrollable immune-related adverse events remain a major challenge. In this study, we developed a tumor-activated nanoparticle that is specifically active in tumors but not in normal tissues. We discovered a short anti-PD-L1 peptide that blocks the PD-1/PD-L1 interaction.
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