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Physical Sciences and Mathematics Commons™
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- CMMB (3)
- Amyloid former (1)
- Anti-bacterial (1)
- Antimalarial (1)
- Biindole (1)
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- Chaperone (1)
- Circular dichroism (1)
- Cyclic peptide (1)
- Cyclic peptoid (1)
- Diaminopyrimidine (1)
- Mass spectrometry (1)
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- Neutron (1)
- Oxidative dimerisation (1)
- Peptide macrocycles (1)
- Protein dynamics (1)
- Protein folding (1)
- RCM (1)
- Small heat shock protein (1)
- Structure-activity relationship (1)
- Thallium oxidative coupling (1)
Articles 1 - 5 of 5
Full-Text Articles in Physical Sciences and Mathematics
Dynamics Of Apomyoglobin In The Α-To-Β Transition And Of Partially Unfolded Aggregated Protein, E. Fabiani, A. M. Stadler, D. Madern, M. M. Koza, M. Tehei, M. Hirai, G. Zaccai
Dynamics Of Apomyoglobin In The Α-To-Β Transition And Of Partially Unfolded Aggregated Protein, E. Fabiani, A. M. Stadler, D. Madern, M. M. Koza, M. Tehei, M. Hirai, G. Zaccai
Faculty of Science - Papers (Archive)
Changes of molecular dynamics in the α-to-β transition associated with amyloid fibril formation were explored on apo-myoglobin (ApoMb) as a model system. Circular dichroism, neutron and X-ray scattering experiments were performed as a function of temperature on the protein, at different solvent conditions. A significant change in molecular dynamics was observed at the α-to-β transition at about 55 ˚C, indicating a more resilient high temperature β structure phase. A similar effect at approximately the same temperature was observed in holo-myoglobin, associated with partial unfolding and protein aggregation. A study in a wide temperature range between 20 K and 360 K …
Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina
Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina
Faculty of Science - Papers (Archive)
The alpha-crystallins are members of the small heat shock protein (sHSP) family of molecular chaperones which have evolved to minimize intracellular protein aggregation, however they are also implicated in a number of protein deposition diseases. In this study we have employed novel mass spectrometry techniques to investigate the changes in quaternary structure associated with this switch from chaperone to adjuvant of aggregation. We have replicated the oligomeric rearrangements observed for in vivo disease-related modifications, without altering the protein sequence, by refolding the alpha-crystallins in vitro. This refolding results in a loss of dimeric substructure concomitant with an augmentation of substrate …
Antimalarial Activity Of 2,4-Diaminopyrimidines, J. Morgan, R. Haritakul, Paul A. Keller
Antimalarial Activity Of 2,4-Diaminopyrimidines, J. Morgan, R. Haritakul, Paul A. Keller
Faculty of Science - Papers (Archive)
A series of 2,4- and 4,6-diaminopyrimidines were prepared and evaluated for their in vitro antimalarial activity. Of the 12 compounds tested 7 showed reasonable activity with 1 having a sub-micromolar IC50.
New Cyclic Peptides Via Ring-Closing Metathesis Reactions And Their Anti-Bacterial Activities, Timothy P. Boyle, John B. Bremner, Jonathan Coates, John Deadman, Paul A. Keller, Stephen G. Pyne, David I. Rhodes
New Cyclic Peptides Via Ring-Closing Metathesis Reactions And Their Anti-Bacterial Activities, Timothy P. Boyle, John B. Bremner, Jonathan Coates, John Deadman, Paul A. Keller, Stephen G. Pyne, David I. Rhodes
Faculty of Science - Papers (Archive)
As part of a program investigating cyclic peptides with an internal aromatic hydrophobic scaffold as potential novel anti-bacterial agents, we explored the synthesis of simple tyrosine-based systems. These were prepared via key intermediates containing internal allylglycine and allyltyrosine residues for subsequent ring closing metathesis reactions. Although the resulting anti-bacterial activity against Staphylococcus aureus was modest, this represents a novel and simple route to this class of compounds. One intermediate acyclic dipeptide precursor showed good activity against S. aureus with an MIC of 7.8 µg/mL.
Oxidative Coupling Of Indoles Using Thallium(Iii) Trifluoroacetate, Paul A. Keller, N. R. Yepuri, M. J. Kelso, M. Mariani, B. W. Skelton, A. H. White
Oxidative Coupling Of Indoles Using Thallium(Iii) Trifluoroacetate, Paul A. Keller, N. R. Yepuri, M. J. Kelso, M. Mariani, B. W. Skelton, A. H. White
Faculty of Science - Papers (Archive)
The oxidative coupling of polysubstituted electron-rich indoles mediated by thallium trifluoroacetate was found to be a facile, clean, and high yielding reaction. Indolic coupling sites were determined by the nature of the substituents present, with dimerisation at the indole 2-position being the dominant outcome. Indoles bearing two potential reaction sites with similar reactivity were additionally found to undergo heterocoupling.