Results 51 to 60 of about 4,975,440 (284)
Self-Assembly of a Dentinogenic Peptide Hydrogel [PDF]
ACS Omega, 2018 Abstract Current standard of care for treating infected dental pulp, root canal therapy, retains the physical properties of the tooth to a large extent, but does not aim to rejuvenate the pulp tissue. Tissue-engineered acellular biomimetic hydrogels have great potential to facilitate the regeneration of the tissue through the ...
Peter K. Nguyen +7 more
openaire +3 more sources
Structure‐forward targeting of claudins with synthetic binders
FEBS Letters, EarlyView.Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley +1 more source
Peptide-directed self-assembly of hydrogels [PDF]
Acta Biomaterialia, 2009 This review focuses on the self-assembly of macromolecules mediated by the biorecognition of peptide/protein domains. Structures forming alpha-helices and beta-sheets have been used to mediate self-assembly into hydrogels of peptides, reactive copolymers and peptide motifs, block copolymers, and graft copolymers.
Jindrich, Kopecek, Jiyuan, Yang
openaire +2 more sources
Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
FEBS Letters, EarlyView.Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang +2 more
wiley +1 more source
Emerging experimental and computational methods for studying redox‐regulated structural transitions
FEBS Letters, EarlyView.Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
Biomedical Applications of Self-Assembling Peptides
Bioconjugate Chemistry, 2015 Self-assembling peptides have gained increasing attention as versatile molecules to generate diverse supramolecular structures with tunable functionality. Because of the possibility to integrate a wide range of functional domains into self-assembling peptides including cell attachment sequences, signaling domains, vaccine epitopes, and even therapeutic
Radmalekshahi, Mazda +4 more
openaire +4 more sources
FEBS Letters, EarlyView.Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell +2 more
wiley +1 more source
Self-Assembly of Giant Peptide Nanobelts [PDF]
Nano Letters, 2009 Many alkylated peptide amphiphiles have been reported to self-assemble into cylindrical nanofibers with diameters on the order of a few nanometers and micrometer scale lengths; these nanostructures can be highly bioactive and are of great interest in many biomedical applications.
Honggang, Cui +3 more
openaire +2 more sources
Cellular Membrane Enrichment of Self-Assembling d‑Peptides for Cell Surface Engineering
, 2016 We occasionally found that several self-assembling peptides containing d-amino acids would be preferentially enriched in cellular membranes at self-assembled stages while distributed evenly in the cytoplasma of cells at unassembled stages.
Aitian Han (1787499) +7 more
core +1 more source
FEBS Letters, EarlyView.Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley +1 more source