Adekunle Aina

Adekunle Aina
University of British Columbia - Vancouver | UBC · Department of Physics and Astronomy

Doctor of Philosophy

About

11
Publications
448
Reads
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14
Citations
Citations since 2017
11 Research Items
14 Citations
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20172018201920202021202220230123456
20172018201920202021202220230123456
Introduction
Research Scienst | University of British Columbia
Additional affiliations
September 2016 - present
Memorial University of Newfoundland
Position
  • Research Assistant
Description
  • *Teaching first-year Physics 1020 and Physics 1021 *Assessing students’ laboratory reports *Marking and correcting students’ assignments *Invigilating and grading midterm and final exams
September 2016 - present
Memorial University of Newfoundland
Position
  • Research Assistant
Description
  • I am generally interested in computational soft matter and biophysics. Under the supervision of Dr Stefan Wallin at Memorial University, I currently use Monte Carlo-based methods with a coarse-grained model to study proteins.
Education
September 2016 - August 2018
December 2009 - April 2014
University of Lagos
Field of study
  • Physics

Publications

Publications (11)
Article
The profile of shapes presented by a cyclic peptide modulates its therapeutic efficacy and is represented by the ensemble of its sampled conformations. Although some algorithms excel at creating a diverse ensemble of cyclic peptide conformations, they seldom address the entropic contribution of flexible conformations and often have significant prac...
Preprint
Full-text available
Cyclic peptides naturally occur as antibiotics, fungicides, and immunosuppressants, and have been adapted for use as potential therapeutics. Scaffolded cyclic peptide antigens have many protein characteristics such as reduced toxicity, increased stability over linear peptides, and conformational selectivity, but with fewer amino acids than whole pr...
Article
Full-text available
Misfolded toxic forms of alpha-synuclein (α-Syn) have been implicated in the pathogenesis of synucleinopathies, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). The α-Syn oligomers and soluble fibrils have been shown to mediate neurotoxicity and cell-to-cell propagation of pathology. To generat...
Article
Effectively presenting epitopes on immunogens, in order to raise conformationally selective antibodies through active immunization, is a central problem in treating protein misfolding diseases, particularly neurodegenerative diseases such as Alzheimer's disease or Parkinson's disease. We seek to selectively target conformations enriched in toxic, o...
Article
Background: Misfolded, toxic aggregates of proteins capable of prion-like propagation from cell to cell have been implicated in the pathogenesis of neurodegenerative disorders. For example, toxic oligomers of amyloid-beta (Abeta) as well as oligomers and small soluble fibrils of tau and alpha-synuclein (Asyn) have been reported to contribute to ne...
Preprint
Full-text available
Effectively presenting epitopes on immunogens, in order to raise conformationally selective antibodies through active immunization, is a central problem in treating protein misfolding diseases, particularly neurodegenerative diseases such as Alzheimer’s disease or Parkinson’s disease. We seek to selectively target conformations enriched in toxic, o...
Article
Tauopathies are neurodegenerative disorders characterized by the abnormal aggregation of tau protein in the brain. Soluble toxic tau aggregates have the ability to transfer from cell‐to‐cell and to induce newly formed aggregates in recipient cells, thereby propagating tau pathology across the brain in a prion‐like manner. We used computational mode...
Article
Previous studies of Alzheimer’s disease (AD) pathology point to cytotoxic tau as a cause of neuronal cell death, which is induced or exacerbated by soluble misfolded Aβ oligomers. Soluble misfolded species of both tau and Aβ are both observed to propagate cell‐to‐cell. A method for identifying antibodies to tau and Aβ that are conformationally‐sele...
Article
RfaH is a compact two‐domain bacterial transcription factor that functions both as a regulator of transcription and an enhancer of translation. Underpinning the dual functional roles of RfaH is a partial but dramatic fold switch, which completely transforms the ~50‐amino acid C‐terminal domain (CTD) from an all‐α state to an all‐β state. The fold s...
Article
Full-text available
We consider a generalized-ensemble algorithm for coarse-grained simulations of biomolecules which allows the thermodynamic behavior of two or more sequences to be determined in a single mul-tisequence run. By carrying out a random walk in sequence space, the method also enhances conformational sampling. Escape from local energy minima is accelerate...

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