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1. Anatomy of a selectively coassembled β-sheet peptide nanofiber

   https://doi.org/10.1073/pnas.1912810117  

   Shao, Qing; Wong, Kong M.; Seroski, Dillon T.; Wang, Yiming; Liu, Renjie; Paravastu, Anant K.; Hudalla, Gregory A.; Hall, Carol K. (February 2020, Proceedings of the National Academy of Sciences)

   Peptide self-assembly, wherein molecule A associates with other A molecules to form fibrillar β-sheet structures, is common in nature and widely used to fabricate synthetic biomaterials. Selective coassembly of peptide pairs A and B with complementary partial charges is gaining interest due to its potential for expanding the form and function of biomaterials that can be realized. It has been hypothesized that charge-complementary peptides organize into alternating ABAB-type arrangements within assembled β-sheets, but no direct molecular-level evidence exists to support this interpretation. We report a computational and experimental approach to characterize molecular-level organization of the established peptide pair, CATCH. Discontinuous molecular dynamics simulations predict that CATCH(+) and CATCH(−) peptides coassemble but do not self-assemble. Two-layer β-sheet amyloid structures predominate, but off-pathway β-barrel oligomers are also predicted. At low concentration, transmission electron microscopy and dynamic light scattering identified nonfibrillar ∼20-nm oligomers, while at high concentrations elongated fibers predominated. Thioflavin T fluorimetry estimates rapid and near-stoichiometric coassembly of CATCH(+) and CATCH(−) at concentrations ≥100 μM. Natural abundance¹³C NMR and isotope-edited Fourier transform infrared spectroscopy indicate that CATCH(+) and CATCH(−) coassemble into two-component nanofibers instead of self-sorting. However,¹³C–¹³C dipolar recoupling solid-state NMR measurements also identify nonnegligible AA and BB interactions among a majority of AB pairs. Collectively, these results demonstrate that strictly alternating arrangements of β-strands predominate in coassembled CATCH structures, but deviations from perfect alternation occur. Off-pathway β-barrel oligomers are also suggested to occur in coassembled β-strand peptide systems. 

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2. Engineering β-Sheet Peptide Coassemblies for Biomaterial Applications

   https://doi.org/10.1021/acs.jpcb.1c04873  

   Wong, Kong M.; Robang, Alicia S.; Lint, Annabelle H.; Wang, Yiming; Dong, Xin; Xiao, Xingqing; Seroski, Dillon T.; Liu, Renjie; Shao, Qing; Hudalla, Gregory A.; et al (December 2021, The Journal of Physical Chemistry B)
3. Synthesis and β-sheet propensity of constrained N -amino peptides

   https://doi.org/10.1016/j.bmc.2017.08.017  

   Sarnowski, Matthew P.; Pedretty, Kyle P.; Giddings, Nicole; Woodcock, H. Lee; Del Valle, Juan R. (March 2018, Bioorganic & Medicinal Chemistry)
4. De novo design of peptides that coassemble into β sheet–based nanofibrils

   https://doi.org/10.1126/sciadv.abf7668  

   Xiao, Xingqing; Wang, Yiming; Seroski, Dillon T.; Wong, Kong M.; Liu, Renjie; Paravastu, Anant K.; Hudalla, Gregory A.; Hall, Carol K. (September 2021, Science Advances)

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5. Cooperative β-sheet coassembly controls intermolecular orientation of amphiphilic peptide-polydiacetylene conjugates

   https://doi.org/10.1016/j.ssnmr.2024.101959  

   Sudarshan, Tarunya Rao; Lim, Sujeung; Li, Jeffrey; Robang, Alicia S; Liberty, Leel Mazal; Ardoña, Herdeline_Ann M; Paravastu, Anant K (October 2024, Solid State Nuclear Magnetic Resonance)