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Appella D.H., Christianson L.A., Klein D.A., Powell D.R., Huang X., Barchi J.J. Jr., Gellman S.H. Residue-based control of helix shape in β-peptide oligomers. Nature. 387:1997;381-384.
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(1997)
Nature
, vol.387
, pp. 381-384
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Appella, D.H.1
Christianson, L.A.2
Klein, D.A.3
Powell, D.R.4
Huang, X.5
Barchi J.J., Jr.6
Gellman, S.H.7
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46
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0033577324
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Formation of short, stable helices in aqueous solution by β-amino acid hexamers
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The solution structures of water-soluble β-peptide hexamers were studied. These polycationic compounds are synthesized with specific sequences of diverse cyclohexyl and acyclic residues. A high-resolution structure, the first for an unnatural oligomer in aqueous solution, is obtained by two-dimensional NMR spectroscopy and reveals a '14-helix'
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Appella D.H., Barchi J.J. Jr., Durell S.R., Gellman S.H. Formation of short, stable helices in aqueous solution by β-amino acid hexamers. J Am Chem Soc. 121:1999;2309-2310. The solution structures of water-soluble β-peptide hexamers were studied. These polycationic compounds are synthesized with specific sequences of diverse cyclohexyl and acyclic residues. A high-resolution structure, the first for an unnatural oligomer in aqueous solution, is obtained by two-dimensional NMR spectroscopy and reveals a '14-helix'.
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(1999)
J Am Chem Soc
, vol.121
, pp. 2309-2310
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Appella, D.H.1
Barchi J.J., Jr.2
Durell, S.R.3
Gellman, S.H.4
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47
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0033532930
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Synthesis and characterization of trans-2-aminocyclohexanecarboxylic acid oligomers: An unnatural helical secondary structure and implications for β-peptide tertiray structure
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Appella D., Christianson L., Karle I., Powell D., Gellman S. Synthesis and characterization of trans-2-aminocyclohexanecarboxylic acid oligomers: an unnatural helical secondary structure and implications for β-peptide tertiray structure. J Am Chem Soc. 121:1999;6206-6212.
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(1999)
J Am Chem Soc
, vol.121
, pp. 6206-6212
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Appella, D.1
Christianson, L.2
Karle, I.3
Powell, D.4
Gellman, S.5
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48
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0000333938
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3-amino acids and their use as building blocks for the solid-phase synthesis of β-peptides
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3-amino acids and their use as building blocks for the solid-phase synthesis of β-peptides. Helv Chim Acta. 80:1998;187-206.
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(1998)
Helv Chim Acta
, vol.80
, pp. 187-206
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Guichard, G.1
Abele, S.2
Seebach, D.3
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49
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0032811713
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EPC-Synthesis of β-amino acid derivatives through lithiated hydropyrimidines
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Seebach D., Boog A., Schweizer W.B. EPC-Synthesis of β-amino acid derivatives through lithiated hydropyrimidines. Eur J Org Chem. 1999;335-360.
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(1999)
Eur J Org Chem
, pp. 335-360
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Seebach, D.1
Boog, A.2
Schweizer, W.B.3
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50
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0001452530
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3-peptides with proteinaceous side chains: Synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding
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3-peptides with proteinaceous side chains: synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding. Helv Chim Acta 1998. 81:0042;932-982.
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Helv Chim Acta 1998
, vol.81
, pp. 932-982
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Seebach, D.1
Abele, S.2
Gademann, K.3
Guichard, G.4
Hintermann, T.5
Jaun, B.6
Matthews, J.L.7
Schreiber, J.V.8
Oberer, L.9
Hommel, U.10
Widmer, H.11
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51
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0032431413
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3,3-amino acids: A turn motif for β-peptides
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3,3-amino acids: a turn motif for β-peptides. Helv Chim Acta 1998. 81:0042;2218-2243.
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Helv Chim Acta 1998
, vol.81
, pp. 2218-2243
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Seebach, D.1
Abele, S.2
Sifferlen, T.3
Hanggi, M.4
Gruner, S.5
Seiler, P.6
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52
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0032918845
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Temperature-dependent, NMR and CD spectra of β-peptides: On the thermal stability of β-peptide helices - is the folding process of β-peptides non-cooperative?
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Gademann K., Jaun B., Seebach D., Perozzo R., Scapozza L., Folkers G. Temperature-dependent, NMR and CD spectra of β-peptides: on the thermal stability of β-peptide helices - is the folding process of β-peptides non-cooperative? Helv Chim Acta. 82:1999;1-11.
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(1999)
Helv Chim Acta
, vol.82
, pp. 1-11
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Gademann, K.1
Jaun, B.2
Seebach, D.3
Perozzo, R.4
Scapozza, L.5
Folkers, G.6
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53
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0033153367
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Pleated sheets and turns of β-peptides with proteinogenic side chains
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Seebach D., Abele S., Gademann K., Jaun B. Pleated sheets and turns of β-peptides with proteinogenic side chains. Angew Chem Int Ed. 38:1999;1595-1597.
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(1999)
Angew Chem Int Ed
, vol.38
, pp. 1595-1597
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Seebach, D.1
Abele, S.2
Gademann, K.3
Jaun, B.4
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55
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0033519190
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Synthesis and biological evaluation of a cyclo-β-peptide as a somatostatin analog
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A cyclic β-tetrapeptide is found to bind to somatostatin receptors with micromolar affinity - a weak binding affinity compared with the low-nanomolar affinity of natural somatostatin. The β-peptide was modeled on octeotride, a cyclic peptide that is used clinically as an acromegaly and intestinal cancer treatment. Results are taken as evidence that β-peptides may constitute a general scaffold for generating molecules that function as agonists or antagonists of natural peptides
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Gademann K., Ernst M., Hoyer D., Seebach D. Synthesis and biological evaluation of a cyclo-β-peptide as a somatostatin analog. Agnew Chem Int Ed. 38:1999;1223-1226. A cyclic β-tetrapeptide is found to bind to somatostatin receptors with micromolar affinity - a weak binding affinity compared with the low-nanomolar affinity of natural somatostatin. The β-peptide was modeled on octeotride, a cyclic peptide that is used clinically as an acromegaly and intestinal cancer treatment. Results are taken as evidence that β-peptides may constitute a general scaffold for generating molecules that function as agonists or antagonists of natural peptides.
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(1999)
Agnew Chem Int Ed
, vol.38
, pp. 1223-1226
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Gademann, K.1
Ernst, M.2
Hoyer, D.3
Seebach, D.4
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56
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0032569174
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Design of secondary structures in unnatural peptides: Stable helical γ-tetra-, hexa-, and octapeptides and consequences of α-substitution
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γ-Peptide tetramer, hexamer, and octamer sequences are derived by homologation of L-alanine and L-valine. Two-dimensional NMR studies of these molecules in pyridine solution show the presence of stable secondary structure, even at the tetramer length. The conformation is defined by 14-membered hydrogen-bonded rings, creating right-handed helices with a pitch of ~ 5 Å. The structure appears to be stable at 323K
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Hanessian S., Luo X., Schaum R., Michnick S. Design of secondary structures in unnatural peptides: stable helical γ-tetra-, hexa-, and octapeptides and consequences of α-substitution. J Am Chem Soc. 120:1998;8569-8570. γ-Peptide tetramer, hexamer, and octamer sequences are derived by homologation of L-alanine and L-valine. Two-dimensional NMR studies of these molecules in pyridine solution show the presence of stable secondary structure, even at the tetramer length. The conformation is defined by 14-membered hydrogen-bonded rings, creating right-handed helices with a pitch of ~ 5 Å. The structure appears to be stable at 323K.
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(1998)
J Am Chem Soc
, vol.120
, pp. 8569-8570
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Hanessian, S.1
Luo, X.2
Schaum, R.3
Michnick, S.4
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57
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0001000382
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2-OH
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A γ-peptide hexamer containing valine, alanine and leucine sidechains was studied and compared with the corresponding α-peptides and β-peptides. A stable secondary structure for the γ-peptide is characterized by two-dimensional NMR spectroscopy in organic solvents. A right-handed helical structure is described with a pitch of 5 Å, and defined by the formation of 14-membered hydrogen-bonded rings along the backbone
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2-OH. Helv Chim Acta. 81:1998;983-1002. A γ-peptide hexamer containing valine, alanine and leucine sidechains was studied and compared with the corresponding α-peptides and β-peptides. A stable secondary structure for the γ-peptide is characterized by two-dimensional NMR spectroscopy in organic solvents. A right-handed helical structure is described with a pitch of 5 Å, and defined by the formation of 14-membered hydrogen-bonded rings along the backbone.
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(1998)
Helv Chim Acta
, vol.81
, pp. 983-1002
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Hintermann, T.1
Gademann, K.2
Jaun, B.3
Seebach, D.4
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58
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0033516710
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Synthesis and folding preferences of gamma-amino acid oligopeptides: Stereochemical control in the formation of a reverse turn and a helix
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Hanessian S., Luo X.H., Schaum R. Synthesis and folding preferences of gamma-amino acid oligopeptides: stereochemical control in the formation of a reverse turn and a helix. Tetrahedron Lett. 40:1999;4925-4929.
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(1999)
Tetrahedron Lett
, vol.40
, pp. 4925-4929
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Hanessian, S.1
Luo, X.H.2
Schaum, R.3
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59
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0032515982
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Sequence-specific polypeptoids: A diverse family of heteropolymers with stable secondary structure
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Sequence-specific N-substituted glycine polymers (peptoids) up to 36 residues in length were synthesized using a robotic solid-phase protocol. A diverse set of chiral sidechains were incorporated, including aliphatic, aromatic, heterocyclic, cationic and anionic groups. CD spectra indicative of helical secondary structures are observed in both aqueous and organic solvents at temperatures up to 65°C. This structure is stable at short chain lengths (5 residues), despite the inability of these molecules to form backbone hydrogen bonds
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Kirshenbaum K., Barron A.E., Goldsmith R.E., Armand P.A., Bradley E.K., Truong K.T.V., Dill K.A., Cohen F.E., Zuckermann R.N. Sequence-specific polypeptoids: a diverse family of heteropolymers with stable secondary structure. Proc Natl Acad Sci USA. 95:1998;4303-4308. Sequence-specific N-substituted glycine polymers (peptoids) up to 36 residues in length were synthesized using a robotic solid-phase protocol. A diverse set of chiral sidechains were incorporated, including aliphatic, aromatic, heterocyclic, cationic and anionic groups. CD spectra indicative of helical secondary structures are observed in both aqueous and organic solvents at temperatures up to 65°C. This structure is stable at short chain lengths (5 residues), despite the inability of these molecules to form backbone hydrogen bonds.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 4303-4308
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Kirshenbaum, K.1
Barron, A.E.2
Goldsmith, R.E.3
Armand, P.A.4
Bradley, E.K.5
Truong, K.T.V.6
Dill, K.A.7
Cohen, F.E.8
Zuckermann, R.N.9
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60
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13144306061
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NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains
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Armand P., Kirshenbaum K., Goldsmith R.A., Farr-Jones S., Barron A.E., Truong K.T.V., Dill K.A., Mierke D.F., Cohen F.E., Zuckermann R.N.et al. NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains. Proc Natl Acad Sci USA. 95:1998;4309-4314.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 4309-4314
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Armand, P.1
Kirshenbaum, K.2
Goldsmith, R.A.3
Farr-Jones, S.4
Barron, A.E.5
Truong, K.T.V.6
Dill, K.A.7
Mierke, D.F.8
Cohen, F.E.9
Zuckermann, R.N.10
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61
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0032539598
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A combinatorial approach to the discovery of efficient cationic peptoid reagents for gene delivery
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Murphy J.E., Uno T., Hamer J.D., Cohen F.E., Dwarki V., Zuckermann R.N. A combinatorial approach to the discovery of efficient cationic peptoid reagents for gene delivery. Proc Natl Acad Sci USA. 95:1998;1517-1522.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 1517-1522
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Murphy, J.E.1
Uno, T.2
Hamer, J.D.3
Cohen, F.E.4
Dwarki, V.5
Zuckermann, R.N.6
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62
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0033608075
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Novel turns and helices in peptides of chiral α-aminoxy acids
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Yang D., Qu J., Li B., Ng F., Wang X., Cheung K., Wang D., Wu Y. Novel turns and helices in peptides of chiral α-aminoxy acids. J Am Chem Soc. 121:1999;589-590.
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(1999)
J Am Chem Soc
, vol.121
, pp. 589-590
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Yang, D.1
Qu, J.2
Li, B.3
Ng, F.4
Wang, X.5
Cheung, K.6
Wang, D.7
Wu, Y.8
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63
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0033574619
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Submonomer solution synthesis of hydrazinoazapeptoids, a new class of pseudopeptides
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Cheguillaume A., Lehardy F., Bouget K., Baudy-Floc'h M., Le Grel P. Submonomer solution synthesis of hydrazinoazapeptoids, a new class of pseudopeptides. J Org Chem. 64:1999;2924-2927.
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(1999)
J Org Chem
, vol.64
, pp. 2924-2927
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Cheguillaume, A.1
Lehardy, F.2
Bouget, K.3
Baudy-Floc'h, M.4
Le Grel, P.5
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