De Novo Design, Synthesis, and Mechanistic Evaluation of Short Peptides That Mimic Heat Shock Protein 27 Activity

Autor: Jessica Kho, Suhyeon Kwon, Heath Ecroyd, P Chi Pham, Huixin Wang, Shelli R McAlpine, Alana Y Huang, W Alexander Donald, Joel P Rivers

Publikováno v: ACS Med Chem Lett

[Image: see text] We report the first small molecule peptides based on the N-terminal sequence of heat shock protein 27 (Hsp27, gene HSPB1) that demonstrates chaperone-like activity. The peptide, comprising the SWDPF sequence located at Hsp27’s ami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d09a41c52f679fa3069245c265df54d1
https://doi.org/10.1021/acsmedchemlett.0c00609

Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei

Autor: Daniela Vullo, Sonia Del Prete, Pietro Di Fonzo, Vincenzo Carginale, W. Alexander Donald, Claudiu T. Supuran, Clemente Capasso

Publikováno v: Molecules, Vol 22, Iss 3, p 421 (2017)

We have cloned, purified, and characterized a β-carbonic anhydrase (CA, EC 4.2.1.1), BpsCAβ, from the pathogenic bacterium Burkholderia pseudomallei, responsible for the tropical disease melioidosis. The enzyme showed high catalytic activity for th

Externí odkaz: https://doaj.org/article/34b85e9015c24921a902efb29ccd9537

Ion-Mobility Mass Spectrometry for Chiral Analysis of Small Molecules

Autor: K. M. Mohibul Kabir, W Alexander Donald, J. Diana Zhang

Biological activity can depend strongly on stereoisomerism and enantiomeric states because ligand-binding motifs and the interfaces of protein–protein and protein–biomolecule interactions typically involve chiral centres. For instance, R-thalidom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0ec8be8994f5ed96cfb6835d37b6038a
https://doi.org/10.1016/bs.coac.2018.08.009

Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei

Autor: Vincenzo Carginale, W Alexander Donald, Daniela Vullo, Clemente Capasso, Pietro Di Fonzo, Claudiu T. Supuran, Sonia Del Prete

Publikováno v: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules; Volume 22; Issue 3; Pages: 421
Molecules, Vol 22, Iss 3, p 421 (2017)
Molecules (Basel, Online) 22 (2017). doi:10.3390/molecules22030421
info:cnr-pdr/source/autori:Vullo, Daniela; Del Prete, Sonia; Di Fonzo, Pietro; Carginale, Vincenzo; Donald, W. Alexander; Supuran, Claudiu T.; Capasso, Clemente/titolo:Comparison of the Sulfonamide Inhibition Profiles of the-and-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei/doi:10.3390%2Fmolecules22030421/rivista:Molecules (Basel, Online)/anno:2017/pagina_da:/pagina_a:/intervallo_pagine:/volume:22

We have cloned, purified, and characterized a -carbonic anhydrase (CA, EC 4.2.1.1), BpsCA, from the pathogenic bacterium Burkholderia pseudomallei, responsible for the tropical disease melioidosis. The enzyme showed high catalytic activity for the ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b40321e0d2b919668943540244e14da5
https://pubmed.ncbi.nlm.nih.gov/28272358