The role of primary sequence in helical control compared across short α- and β³-peptides

References

• Bautista, A. D., Craig, C. J., Harker, E. A., & Schepartz, A. (2007). Sophistication of foldamer form and function in vitro and in vivo. Current Opinion in Chemical Biology, 11, 685–692.10.1016/j.cbpa.2007.09.009
   PubMed Web of Science ®Google Scholar
• Chakrabartty, A., Doig, A. J., & Baldwin, R. L. (1993). Helix capping propensities in peptides parallel those in proteins. Proceedings of the National Academy of Sciences, 90, 11332–11336.10.1073/pnas.90.23.11332
   PubMed Web of Science ®Google Scholar
• Chapman, R. N., Dimartino, G., & Arora, P. S. (2004). A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate. Journal of the American Chemical Society, 126, 12252–12253.10.1021/ja0466659
   PubMed Web of Science ®Google Scholar
• Cheng, R. P., Gellman, S. H., & DeGrado, W. F. (2001). β-peptides: From structure to function. Chemical Reviews, 101, 3219–3232.10.1021/cr000045i
   PubMed Web of Science ®Google Scholar
• Ciaccio, N. A., & Laurence, J. S. (2009). Effects of disulfide bond formation and protein helicity on the aggregation of activating transcription factor 5. Molecular Pharmaceutics, 6, 1205–1215.10.1021/mp900058t
   PubMed Web of Science ®Google Scholar
• DeGrado, W. F., Schneider, J. P., & Hamuro, Y. (1999). The twists and turns of beta-peptides. The Journal of Peptide Research, 54, 206–217.
   PubMedGoogle Scholar
• Demizu, Y., Doi, M., Sato, Y., Tanaka, M., Okuda, H., & Kurihara, M. (2010). Three-dimensional structural control of diastereomeric Leu-Leu-Aib-Leu-Leu-Aib sequences in the solid state. The Journal of Organic Chemistry, 75, 5234–5239.10.1021/jo100965r
   PubMed Web of Science ®Google Scholar
• Epand, R. F., Raguse, T. L., Gellman, S. H., & Epand, R. M. (2004). Antimicrobial 14-helical β-peptides: Potent bilayer disrupting agents. Biochemistry, 43, 9527–9535.10.1021/bi049414l
   PubMed Web of Science ®Google Scholar
• Ferrie, J. J., Gruskos, J. J., Goldwaser, A. L., Decker, M. E., & Guarracino, D. A. (2013). A comparative protease stability study of synthetic macrocyclic peptides that mimic two endocrine hormones. Bioorganic & Medicinal Chemistry Letters, 23, 989–995.10.1016/j.bmcl.2012.12.041
   PubMed Web of Science ®Google Scholar
• Forood, B., Feliciano, E. J., & Nambiar, K. P. (1993). Stabilization of α-helical structures in short peptides via end capping. Proceedings of the National Academy of Sciences, 90, 838–842.10.1073/pnas.90.3.838
   PubMed Web of Science ®Google Scholar
• Guarracino, D. A., Chiang, H. R., Banks, T. N., Lear, J. D., Hodsdon, M. E., & Schepartz, A. (2006). Relationship between salt-bridge identity and 14-helix stability of β3-peptides in aqueous buffer. Organic Letters, 8, 807–810.10.1021/ol0527532
   Google Scholar
• Guichard, G., Abele, S., & Seebach, D. (1998). Preparation of N-Fmoc-protected β2- and β3-Amino Acids and their use as building blocks for the solid-phase synthesis of β-peptides. Helvetica Chimica Acta, 81, 187–206.10.1002/(ISSN)1522-2675
   Web of Science ®Google Scholar
• Hart, S. A., Bahadoor, A. B. F., Matthews, E. E., Qiu, X. J., & Schepartz, A. (2003). Helix macrodipole control of β3-peptide 14-helix stability in water. Journal of the American Chemical Society, 125, 4022–4023.10.1021/ja029868a
   PubMed Web of Science ®Google Scholar
• Hoang, H. N., Abbenante, G., Hill, T. A., Ruiz-Gomez, G., & Fairlie, D. P. (2012). Folding pentapeptides into left and right handed alpha helices. Tetrahedron, 68, 4513–4516.10.1016/j.tet.2011.10.108
   Web of Science ®Google Scholar
• Jochim, A. L., & Arora, P. S. (2010). Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitors. ACS Chemical Biology, 5, 919–923.10.1021/cb1001747
   PubMed Web of Science ®Google Scholar
• Kim, Y.-W., Kutchukian, P. S., & Verdine, G. L. (2010). Introduction of all-hydrocarbon i, i+3 staples into α-helices via ring-closing olefin metathesis. Organic Letters, 12, 3046–3049.10.1021/ol1010449
   PubMed Web of Science ®Google Scholar
• Kritzer, J. A., Stephens, O. M., Guarracino, D. A., Reznik, S. K., & Schepartz, A. (2005). β-peptides as inhibitors of protein–protein interactions. Bioorganic & Medicinal Chemistry, 13, 11–16.10.1016/j.bmc.2004.09.009
   PubMed Web of Science ®Google Scholar
• Kritzer, J. A., Tirado-Rives, J., Hart, S. A., Lear, J. D., Jorgensen, W. L., & Schepartz, A. (2005). Relationship between side chain structure and 14-helix stability of β3-peptides in water. Journal of the American Chemical Society, 127, 167–178.10.1021/ja0459375
   Google Scholar
• Maekawa, H., Toniolo, C., Moretto, A., Broxterman, Q. B., & Ge, N.-H. (2006). Different spectral signatures of octapeptide 310- and α-helices revealed by two-dimensional infrared spectroscopy. The Journal of Physical Chemistry B, 110, 5834–5837.10.1021/jp057472q
   PubMed Web of Science ®Google Scholar
• Marqusee, S., Robbins, V. H., & Baldwin, R. L. (1989). Unusually stable helix formation in short alanine-based peptides. Proceedings of the National Academy of Sciences, 86, 5286–5290.10.1073/pnas.86.14.5286
   PubMed Web of Science ®Google Scholar
• Pal, L., Chakrabarti, P., & Basu, G. (2003). Sequence and structure patterns in proteins from an analysis of the shortest helices: Implications for helix nucleation. Journal of Molecular Biology, 326, 273–291.10.1016/S0022-2836(02)01338-4
   PubMed Web of Science ®Google Scholar
• Qiu, J. X., Petersson, E. J., Matthews, E. E., & Schepartz, A. (2006). Toward β-amino acid proteins: A cooperatively folded β-peptide quaternary structure. Journal of the American Chemical Society, 128, 11338–11339.10.1021/ja063164+
   PubMed Web of Science ®Google Scholar
• Sadowsky, J. D., Schmitt, M. A., Lee, H.-S., Umezawa, N., Wang, S., Tomita, Y., & Gellman, S. H. (2005). Chimeric (α/β + α)-peptide ligands for the BH3-recognition clef of Bcl-xL: Critical role of the molecular scaffold in protein surface recognition. Journal of the American Chemical Society, 127, 11966–11968.10.1021/ja053678t
   PubMed Web of Science ®Google Scholar
• Scholtz, J. M., & Baldwin, R. L. (1992). The mechanism of α-helix formation by peptides. Annual Review of Biophysics and Biomolecular Structure, 21, 95–118.10.1146/annurev.bb.21.060192.000523
   PubMedGoogle Scholar
• Sommese, R. F., Sivaramakrishnan, S., Baldwin, R. L., & Spudich, J. A. (2010). Helicity of short E-R/K peptides. Protein Science, 19, 2001–2005.10.1002/pro.469
   PubMed Web of Science ®Google Scholar