Malnutrition Among Older Adults: The Role of Occupational Therapy

Johnson, Michaela E.; Janssen, Sclinda

doi:10.7138/otp.2018.2303.f2

Cited by 1 publication

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“…helix formation) upon binding, which may relieve some fluorescence quenching of the fluorophore. 49,50 For SPR, m 7 GDP-bound eIF4E was immobilized on a HisCap sensor chip (ForteBio) via its N-terminal His 10 tag. 4E-BP1 or eIF4G peptide (12.5-200 nM) was then flowed over the immobilized protein.…”

Section: Kinetic Analysis Of Linear 4e-bp1 and Eif4g Peptidesmentioning

confidence: 99%

Consideration of Binding Kinetics in the Design of Stapled Peptide Mimics of the Disordered Proteins Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 and Eukaryotic Translation Initiation Factor 4G

et al. 2019

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Protein disorder plays a crucial role in signal transduction and is key for many cellular processes including transcription, translation, and cell cycle. Within the intrinsically disordered protein interactome, the α-helix is commonly used for binding, which is induced via a disorder-to-order transition. Because the targeting of protein-protein interactions (PPIs) remains an important challenge in medicinal chemistry, efforts have been made to mimic this secondary structure for rational inhibitor design through the use of stapled peptides. Cap-dependent mRNA translation is regulated by two disordered proteins, 4E-BP1 and eIF4G, that inhibit or stimulate the activity of the m 7 G cap-binding translation initiation factor, eIF4E, respectively. Both use an α-helical motif for eIF4E binding, warranting the investigation of stapled peptide mimics for manipulating eIF4E PPIs. Herein, we describe our efforts toward this goal, resulting in the synthesis of a cell-active stapled peptide for further development in manipulating aberrant cap-dependent translation in human diseases.

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Section: Kinetic Analysis Of Linear 4e-bp1 and Eif4g Peptidesmentioning

confidence: 99%