Results 51 to 60 of about 1,046,387 (249)

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

Structure and assembly of designed β-hairpin peptides in crystals as models for β-sheet aggregation

open access: yes, 2004
De novo designed β-hairpin peptides have generally been recalcitrant to crystallization. The crystal structures of four synthetic peptide β-hairpins, Boc-Leu-Val-Val-dPro-Gly-Leu-Phe-Val-OMe (1), Boc-Leu-Phe-Val-dPro-Ala-Leu-Phe-Val-OMe (2), Boc-Leu-Val ...
Shamala, Narayanaswamy   +4 more
core   +1 more source

Dual Role of Tamoxifen in Enhancing STING and CEACAM1 Expression to Prime a Favorable Tumor Microenvironment for Anti‐TIM3 Immunotherapy

open access: yesAdvanced Science, EarlyView.
Anti‐PD‐1/PD‐L1 blockade has revolutionized cancer immunotherapy, but is ineffective against endocrine‐treated (i.e., Tamoxifen), relapsed ER+ breast cancer (BC) patients. This study provides insight into the sub‐optimal response of ER+BCs to anti‐PD‐1/PD‐L1 blockade – highlighting the induction of STING and the CEACAM1/TIM3 axis after chronic ...
Marvin Angelo E Aberin   +20 more
wiley   +1 more source

Remote Residue Substitution and Macrocyclization Preorganize a β‐Hairpin Peptide and Enhance β‐Catenin Binding

open access: yesChemistryEurope
Peptide‐based inhibitors are promising tools to target challenging protein interfaces, yet improving their affinity and drug‐like properties is still a major hurdle.
Michael H. N. Meulendijks   +11 more
doaj   +1 more source

Aza-Amino Acids Disrupt β-Sheet Secondary Structures

open access: yesMolecules, 2019
Cα to N substitution in aza-amino acids imposes local conformational constraints, changes in hydrogen bonding properties, and leads to adaptive chirality at the nitrogen atom. These properties can be exploited in mimicry and stabilization of peptide
Michael A. McMechen   +3 more
doaj   +1 more source

Effects of As(III) Binding on β-Hairpin Structure

open access: yes, 2016
While arsenic(III) compounds can exert profound toxicological and pharmacological effects, their modes of action and, in particular, the structural consequences of their binding to cysteinyl side chains in proteins, remain poorly understood.
Joel P. Schneider (1532557)   +4 more
core   +1 more source

DNA-Hairpin-Templated Silver Nanoclusters: A Study on Stem Sequence

open access: yes, 2020
DNA hairpins are widely used to synthesize silver nanoclusters (AgNCs) with excellent optical properties due to their specific secondary structure. Hairpin-AgNCs have been popularly employed for sensoring applications, while no systematic study has been ...
Yahui Guo (7547603)   +8 more
core   +1 more source

The Natural Product Corramycin Acts as a DNA Gyrase Poison and Overcomes Fluoroquinolone Resistance in Mycobacterium tuberculosis

open access: yesAdvanced Science, EarlyView.
Corramycin, a myxobacterial natural product antibiotic, exhibits potent bactericidal activity against multidrug‐resistant Mycobacterium tuberculosis. The compound hijacks bacterial transporters such as BacA and OppABCD to enter the cell and inhibits DNA synthesis through a previously unrecognized mode of DNA gyrase poisoning, locking the enzyme in an ...
Franziska Fries   +25 more
wiley   +1 more source

The Antimicrobial Peptide Capitellacin: Chemical Synthesis of Analogues to Probe the Role of Disulphide Bridges and Their Replacement with Vinyl Sulphides

open access: yesAntibiotics
Capitellacin (1) is a 20-residue antimicrobial β-hairpin, produced by the marine polychaeta (segmented worms) Capitella teletai. Since its discovery in 2020, only very limited studies have been undertaken to understand capitellacin’s structure–activity ...
Oscar A. Shepperson   +3 more
doaj   +1 more source

Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides. [PDF]

open access: yesPLoS Computational Biology, 2013
IAPP, a 37 amino-acid peptide hormone belonging to the calcitonin family, is an intrinsically disordered protein that is coexpressed and cosecreted along with insulin by pancreatic islet β-cells in response to meals.
Chun Wu, Joan-Emma Shea
doaj   +1 more source

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