Changes in β-Lactoglobulin Conformation at the Oil/Water Interface of Emulsions Studied by Synchrotron Radiation Circular Dichroism Spectroscopy

Autor: Bonnie A. Wallace, Leonard Keith Pattenden, Tim J Wooster, Mary Ann Augustin, Marie-Isabel Aguilar, Tzong-Hsien Lee, Andrew J. Miles, Jiali Zhai

Publikováno v: Biomacromolecules. 11:2136-2142

The structure of proteins at interfaces is a key factor determining the stability as well as organoleptic properties of food emulsions. While it is widely believed that proteins undergo conformational changes at interfaces, the measurement of these s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::171d6085d5b1982b203e6dae821fd940
https://doi.org/10.1021/bm100510j

Crystal Structures of Highly Constrained Substrate and Hydrolysis Products Bound to HIV-1 Protease. Implications for the Catalytic Mechanism

Autor: Shu-Hong Hu, Jennifer L. Martin, Terry Walsh, Leonard Keith Pattenden, David P. Fairlie, Joel D. A. Tyndall, Robert Reid, Paul F. Alewood, Dianne Alewood

Publikováno v: Biochemistry. 47:3736-3744

HIV-1 protease is a key target in treating HIV infection and AIDS, with 10 inhibitors used clinically. Here we used an unusual hexapeptide substrate, containing two macrocyclic tripeptides constrained to mimic a beta strand conformation, linked by a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8c35aab61b27a5985da5bf2d16d0f52
https://doi.org/10.1021/bi7023157

Controlled oxidative protein refolding using an ion-exchange column

Autor: Susanna Sj Leong, Leonard Keith Pattenden, Marc Langenhof, Anton P. J. Middelberg

Publikováno v: Journal of Chromatography A. 1069:195-201

Column-based refolding of complex and highly disulfide-bonded proteins simplifies protein renaturation at both preparative and process scale by integrating and automating a number of operations commonly used in dilution refolding. Bovine serum albumi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b87846f42766a1ba02697b474c01e53b
https://doi.org/10.1016/j.chroma.2005.01.063

Synthesis, Stability, Antiviral Activity, and Protease-Bound Structures of Substrate-Mimicking Constrained Macrocyclic Inhibitors of HIV-1 Protease

Autor: Paul F. Alewood, David P. Tyssen, Dianne Alewood, Darren K. Jardine, Jennifer L. Martin, David P. Fairlie, Robert Reid, Douglas A. Bergman, Leonard Keith Pattenden, Margaret R. Passmore, Christopher J. Birch, Belinda Todd, Joel D. A. Tyndall, Darren R. March, Shu-Hong Hu

Publikováno v: Journal of Medicinal Chemistry. 43:3495-3504

Three new peptidomimetics (1-3) have been developed with highly stable and conformationally constrained macrocyclic components that replace tripeptide segments of protease substrates. Each compound inhibits both HIV-1 protease and viral replication (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62fb3e594fc02553e3d05e3e3dcb8f23
https://doi.org/10.1021/jm000013n

Fast membrane association is a crucial factor in the peptide Pep-1 translocation mechanism: a kinetic study followed by surface plasmon resonance

Autor: Miguel A. R. B. Castanho, Sónia Troeira Henriques, Leonard Keith Pattenden, Marie-Isabel Aguilar

Publikováno v: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Biopolymers

© 2010 Wiley Periodicals, Inc.
The use of peptide carriers, termed ‘‘cell-penetrating peptides (CPPs)’’ has attracted much attention due to their potential for cellular delivery of hydrophilic molecules with pharmacological interest, ov

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47152547594adce82644520cbf8349cd
https://hdl.handle.net/10451/7274