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Structure Elucidation and Functional Studies of a Novel β-hairpin Antimicrobial Peptide from the Marine Polychaeta Capitella teleta [PDF]

open access: goldMarine Drugs, 2020
Endogenous antimicrobial peptides (AMPs) are evolutionary ancient molecular factors of innate immunity that play a key role in host defense. Among the most active and stable under physiological conditions AMPs are the peptides of animal origin that adopt
Pavel V. Panteleev   +7 more
doaj   +3 more sources

Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics. [PDF]

open access: greenACS Chem Biol, 2021
β-Strands are a fundamental component of protein structure, and these extended peptide regions serve as binding epitopes for numerous protein-protein complexes.
Blosser SL   +4 more
europepmc   +4 more sources

The β-hairpin of 40S exit channel protein Rps5/uS7 promotes efficient and accurate translation initiation in vivo

open access: goldeLife, 2015
The eukaryotic 43S pre-initiation complex bearing tRNAiMet scans the mRNA leader for an AUG start codon in favorable context. Structural analyses revealed that the β-hairpin of 40S protein Rps5/uS7 protrudes into the 40S mRNA exit-channel, contacting the
Jyothsna Visweswaraiah   +3 more
doaj   +3 more sources

Designing and identifying β-hairpin peptide macrocycles with antibiotic potential. [PDF]

open access: yesSci Adv, 2023
Peptide macrocycles are a rapidly emerging class of therapeutic, yet the design of their structure and activity remains challenging. This is especially true for those with β-hairpin structure due to weak folding properties and a propensity for ...
Randall JR   +8 more
europepmc   +2 more sources

β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides. [PDF]

open access: yesPLoS ONE, 2014
Protein misfolding disorders are associated with conformational changes in specific proteins, leading to the formation of potentially neurotoxic amyloid fibrils. During pathogenesis of prion disease, the prion protein misfolds into β-sheet rich, protease-
Andrew C Gill
doaj   +5 more sources

A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus [PDF]

open access: goldViruses, 2021
Pestivirus envelope protein E2 is crucial to virus infection and accomplishes virus-receptor interaction during entry. However, mapping of E2 residues mediating these interactions has remained unexplored.
Fernando Merwaiss   +5 more
doaj   +2 more sources

Stapled β-Hairpin Antimicrobial Peptides with Improved Stability and Activity against Drug-Resistant Gram-Negative Bacteria. [PDF]

open access: yesJ Med Chem, 2023
Different stapling techniques have been used recently to address the subpar performance of antimicrobial peptides (AMPs) in clinical trials with ample focus on α-helical AMPs. In comparison, a systematic evaluation of such strategies on β-hairpin AMPs is
Selvarajan V   +7 more
europepmc   +2 more sources

De novo design of a nanopore for single-molecule detection that incorporates a β-hairpin peptide. [PDF]

open access: yesNat Nanotechnol, 2022
The amino-acid sequence of a protein encodes information on its three-dimensional structure and specific functionality. De novo design has emerged as a method to manipulate the primary structure for the development of artificial proteins and peptides ...
Shimizu K   +10 more
europepmc   +2 more sources

Mechanism of Action and Therapeutic Potential of the β-Hairpin Antimicrobial Peptide Capitellacin from the Marine Polychaeta Capitella teleta. [PDF]

open access: yesMar Drugs, 2022
Among the most potent and proteolytically resistant antimicrobial peptides (AMPs) of animal origin are molecules forming a β-hairpin structure stabilized by disulfide bonds. In this study, we investigated the mechanism of action and therapeutic potential
Safronova VN   +5 more
europepmc   +2 more sources

Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue. [PDF]

open access: yesJ Am Chem Soc
A family of neurodegenerative diseases, including Huntington’s disease (HD) and spinocerebellar ataxias, are associated with an abnormal polyglutamine (polyQ) expansion in mutant proteins that become prone to form amyloid-like aggregates.
Parlato R   +9 more
europepmc   +2 more sources

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